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Beta-propeller

March 08, 2024

In structural biology, a beta-propeller (β-propeller) is a type of all-β protein architecture characterized by 4 to 8 highly symmetrical blade-shaped beta sheets arranged toroidally around a central axis. Together the beta-sheets form a funnel-like active site.

WD domain, G-beta repeat
Ribbon diagram of the C-terminal WD40 domain of Tup1 (a transcriptional co-repressor in yeast), which adopts a 7-bladed beta-propeller fold. Ribbon is colored from blue (N-terminus) to red (C-terminus). PDB 1erj [1]
Identifiers
SymbolWD40
PfamPF00400
Pfam clanCL0186
InterProIPR001680
PROSITEPDOC00574
SCOP21gp2 / SCOPe / SUPFAM
CDDcd00200
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Structure edit

Each beta-sheet typically has four anti-parallel β-strands arranged in the beta-zigzag motif.[2] The strands are twisted so that the first and fourth strands are almost perpendicular to each other.[3] There are five classes of beta-propellers, each arrangement being a highly symmetrical structure with 4–8 beta sheets, all of which generally form a central tunnel that yields pseudo-symmetric axes.[2]

While, the protein's official active site for ligand-binding is formed at one end of the central tunnel by loops between individual beta-strands, protein-protein interactions can occur at multiple areas around the domain. Depending on the packing and tilt of the beta-sheets and beta-strands, the beta-propeller may have a central pocket in place of a tunnel.[4]

The beta-propeller structure is stabilized mainly through hydrophobic interactions of the beta-sheets, while additional stability may come from hydrogen bonds formed between the beta-sheets of the C- and N-terminal ends. In effect this closes the circle which can occur even more strongly in 4-bladed proteins via a disulfide bond.[2] The chaperones Hsp70 and CCT have been shown to sequentially bind nascent beta-propellers as they emerge from the ribosome. These chaperones prevent non-native inter-blade interactions from forming until the entire beta-propeller is synthesized.[5] Many beta-propellers are dependent on CCT for expression.[6][7][8] In at least one case, ions have been shown to increase stability by binding deep in the central tunnel of the beta-propeller.[4]

Murzin proposed a geometric model to describe the structural principles of the beta propeller.[9] According to this model the seven bladed propeller was the most favored arrangement in geometric terms.

Despite its highly conserved nature, beta-propellers are well known for their plasticity. Beyond having a variety of allowed beta-sheets per domain, it can also accommodate other domains into its beta-sheets. Additionally, there are proteins that have shown variance in the number of beta-strands per beta-sheet. Rather than having the typical four beta-strands in a sheet, beta-lactamase inhibitor protein-II only has three beta-strands per sheet while the phytase of Bacillus subtilis has five beta-strands per beta-sheet.[2]

Function edit

Due to its structure and plasticity, protein-protein interactions can form with the top, bottom, central channel, and side faces of the beta-propeller.[4] The function of the propeller can vary based on the blade number. Four-bladed beta-propellers function mainly as transport proteins, and because of its structure, they have a conformation that is favorable for substrate binding.[4] Unlike larger beta-propellers, four-bladed beta-propellers usually cannot perform catalysis themselves, but act instead to aid in catalysis by performing the aforementioned functions. Five-bladed propellers can act as transferases, hydrolases, and sugar binding proteins.[4] Six- and seven-bladed propellers perform a much broader variety of functions in comparison to four- and five-bladed propellers. These functions can include acting as ligand-binding proteins, hydrolases, lyases, isomerases, signaling proteins, structural proteins, and oxidoreductases.[4]

Variations in the larger (five- to eight-bladed) beta-propellers can allow for even more specific functions. This is the case with the C-terminal region of GyrA which expresses a positively charged surface ideal for binding DNA. Two alpha-helices coming out of the six-bladed beta-propeller of serum paraoxonase may provide a hydrophobic region ideal for anchoring membranes. DNA damage-binding protein 1 has three beta-propellers, in which the connection between two of the propellers is inserted into the third propeller potentially allowing for its unique function.[4]

Clinical Significance edit

  • Beta-propeller protein-associated neurodegeneration (BPAN) is a condition characterized by early onset seizures, developmental delays, and intellectual disability. With aging, muscle and cognitive degeneration may also occur. Variants of the WDR45 gene have been identified in both males and females with this condition.[10]
  • Familial hypercholesterolemia is a human genetic disease caused by mutations to the gene that encodes low density lipoprotein receptor (LDLR), a protein which has at least one beta-propeller. This disease causes increased concentrations of low-density lipoprotein (LDL) and cholesterol which can lead to further consequences such as coronary atherosclerosis. Confirmed mutations have been shown to interfere with hydrogen bonding between blades of the beta-propeller.[2]
  • The beta-propeller has been used in protein engineering in several cases. Yoshida et al., for example, worked with glucose dehydrogenase (GDH), having a six-blade beta-propeller, to make an enzyme ideal for use as a glucose sensor. They succeeded in engineering a GDH chimera which had a higher thermostability, higher co-factor binding stability, and increased substrate specificity. These properties were attributed to increased hydrophobic interactions due to mutations at the C-terminus of the beta-propeller.[2]
  • The beta-propeller domain of the influenza virus neuraminidase are often used for drug design. Through study of this enzyme, researchers have developed influenza neuraminidase inhibitors which effectively block the influenza neuraminidase and consequently slowing or stopping the progression of the influenza infection.[2]

Examples edit

  • The influenza virus protein viral neuraminidase is a six-bladed beta-propeller protein whose active form is a tetramer.[11] It is one of two proteins present in the viral envelope and catalyzes the cleavage of sialic acid moieties from cell-membrane proteins to aid in the targeting of newly produced virions to previously uninfected cells.[12]
  • WD40 repeats, also known as beta-transducin repeats, are short fragments found primarily in eukaryotes.[13][14] They usually form beta-propellers with 7–8 blades, but have also been shown to form structural domains with 4 to 16 repeated units critical for protein–protein interactions. WD40 protein motifs are involved in a variety of functions including signal transduction, transcription regulation, and regulation of the cell cycle. They also work as sites for protein-protein interactions, and can even play a role in the assembly of protein complexes. Specificity of these structural domains are determined by the sequence of the protein outside of itself.[15]
  • A beta-propeller is a critical component of LDLR and aids in a pH based conformational change. At neutral pH the LDLR is in an extended linear conformation and can bind ligands (PCSK9). At acidic pH the linear conformation changes to a hairpin structure such that ligand binding sites bind to the beta-propeller, preventing ligand binding.[16][17]
  • Beta-propeller phytases consist of a six-bladed β-propeller structure. Phytases are phosphatases that can hydrolyze the ester bonds of phytate, the major form of phosphate storage in plants. Through this process, phosphate that is normally inaccessible to livestock becomes available. Most livestock feed has added inorganic phosphate, which when excreted, can cause environmental pollution. The addition of phytase instead of phosphate into livestock feed would allow for animals to break down the phosphate already available in the plant matter. This would theoretically produce less pollution as less of the excess phosphate would be excreted.[18]

Domains edit

Repeat domains known to fold into a beta-propeller include WD40, YWTD, Kelch, YVTN, RIVW (PD40), and many more. Their sequences tend to group together, suggesting a close evolutionary link. They are also related to many beta-containing domains.[19]

References edit

  1. ^ Sprague ER, Redd MJ, Johnson AD, Wolberger C (June 2000). "Structure of the C-terminal domain of Tup1, a corepressor of transcription in yeast". The EMBO Journal. 19 (12): 3016–27. doi:10.1093/emboj/19.12.3016. PMC 203344. PMID 10856245.
  2. ^ a b c d e f g "Beta-propellers: Associated Functions and their Role in Human Diseases". ResearchGate. Retrieved 2018-11-17.
  3. ^ Kuriyan, Konforti, Wemmer, John, Boyana, David (2013). The molecules of life: physical and chemical principles. New York: Garland Science. pp. 163–164. ISBN 9780815341888.{{cite book}}: CS1 maint: multiple names: authors list (link)
  4. ^ a b c d e f g Chen CK, Chan NL, Wang AH (October 2011). "The many blades of the β-propeller proteins: conserved but versatile". Trends in Biochemical Sciences. 36 (10): 553–61. doi:10.1016/j.tibs.2011.07.004. PMID 21924917.
  5. ^ Stein KC, Kriel A, Frydman J (July 2019). "Nascent Polypeptide Domain Topology and Elongation Rate Direct the Cotranslational Hierarchy of Hsp70 and TRiC/CCT". Molecular Cell. 75 (6): 1117–1130.e5. doi:10.1016/j.molcel.2019.06.036. PMC 6953483. PMID 31400849.
  6. ^ Plimpton RL, Cuéllar J, Lai CW, Aoba T, Makaju A, Franklin S, et al. (February 2015). "Structures of the Gβ-CCT and PhLP1-Gβ-CCT complexes reveal a mechanism for G-protein β-subunit folding and Gβγ dimer assembly". Proceedings of the National Academy of Sciences of the United States of America. 112 (8): 2413–8. Bibcode:2015PNAS..112.2413P. doi:10.1073/pnas.1419595112. PMC 4345582. PMID 25675501.
  7. ^ Cuéllar J, Ludlam WG, Tensmeyer NC, Aoba T, Dhavale M, Santiago C, et al. (June 2019). "Structural and functional analysis of the role of the chaperonin CCT in mTOR complex assembly". Nature Communications. 10 (1): 2865. Bibcode:2019NatCo..10.2865C. doi:10.1038/s41467-019-10781-1. PMC 6599039. PMID 31253771.
  8. ^ Ludlam, WG; Aoba, T; Cuéllar, J; Bueno-Carrasco, MT; Makaju, A; Moody, JD; Franklin, S; Valpuesta, JM; Willardson, BM (2019-11-01). "Molecular architecture of the Bardet-Biedl syndrome protein 2-7-9 subcomplex". The Journal of Biological Chemistry. 294 (44): 16385–16399. doi:10.1074/jbc.RA119.010150. hdl:10261/240872. PMC 6827290. PMID 31530639.
  9. ^ Murzin AG (October 1992). "Structural principles for the propeller assembly of beta-sheets: the preference for seven-fold symmetry". Proteins. 14 (2): 191–201. doi:10.1002/prot.340140206. PMID 1409568. S2CID 22228091.
  10. ^ Gregory A, Kurian MA, Haack T, Hayflick SJ, Hogarth P (1993). Adam MP, Ardinger HH, Pagon RA, Wallace SE (eds.). Beta-Propeller Protein-Associated Neurodegeneration. University of Washington, Seattle. PMID 28211668. Retrieved 2018-11-20. {{cite book}}: |work= ignored (help)
  11. ^ Air GM (July 2012). "Influenza neuraminidase". Influenza and Other Respiratory Viruses. 6 (4): 245–56. doi:10.1111/j.1750-2659.2011.00304.x. PMC 3290697. PMID 22085243.
  12. ^ Matrosovich MN, Matrosovich TY, Gray T, Roberts NA, Klenk HD (November 2004). "Neuraminidase is important for the initiation of influenza virus infection in human airway epithelium". Journal of Virology. 78 (22): 12665–7. doi:10.1128/JVI.78.22.12665-12667.2004. PMC 525087. PMID 15507653.
  13. ^ Neer EJ, Schmidt CJ, Nambudripad R, Smith TF (September 1994). "The ancient regulatory-protein family of WD-repeat proteins". Nature. 371 (6495): 297–300. Bibcode:1994Natur.371..297N. doi:10.1038/371297a0. PMID 8090199. S2CID 600856.
  14. ^ Smith TF, Gaitatzes C, Saxena K, Neer EJ (May 1999). "The WD repeat: a common architecture for diverse functions". Trends in Biochemical Sciences. 24 (5): 181–5. doi:10.1016/S0968-0004(99)01384-5. PMID 10322433.
  15. ^ EMBL-EBI, InterPro. "WD40-like Beta Propeller (IPR011659) < InterPro < EMBL-EBI". www.ebi.ac.uk. Retrieved 2018-11-19.
  16. ^ Zhang DW, Garuti R, Tang WJ, Cohen JC, Hobbs HH (September 2008). "Structural requirements for PCSK9-mediated degradation of the low-density lipoprotein receptor". Proceedings of the National Academy of Sciences of the United States of America. 105 (35): 13045–50. Bibcode:2008PNAS..10513045Z. doi:10.1073/pnas.0806312105. PMC 2526098. PMID 18753623.
  17. ^ Betteridge DJ (February 2013). "Cardiovascular endocrinology in 2012: PCSK9-an exciting target for reducing LDL-cholesterol levels". Nature Reviews. Endocrinology. 9 (2): 76–8. doi:10.1038/nrendo.2012.254. PMID 23296165. S2CID 27839784.
  18. ^ Chen CC, Cheng KJ, Ko TP, Guo RT (2015-01-09). "Current Progresses in Phytase Research: Three-Dimensional Structure and Protein Engineering". ChemBioEng Reviews. 2 (2): 76–86. doi:10.1002/cben.201400026.
  19. ^ Kopec KO, Lupas AN (2013). "β-Propeller blades as ancestral peptides in protein evolution". PLOS ONE. 8 (10): e77074. Bibcode:2013PLoSO...877074K. doi:10.1371/journal.pone.0077074. PMC 3797127. PMID 24143202.

Further reading edit

  • Branden C, Tooze J. (1999). Introduction to Protein Structure 2nd ed. Garland Publishing: New York, NY.

External links edit

March 08, 2024
beta, propeller, structural, biology, beta, propeller, propeller, type, protein, architecture, characterized, highly, symmetrical, blade, shaped, beta, sheets, arranged, toroidally, around, central, axis, together, beta, sheets, form, funnel, like, active, sit. In structural biology a beta propeller b propeller is a type of all b protein architecture characterized by 4 to 8 highly symmetrical blade shaped beta sheets arranged toroidally around a central axis Together the beta sheets form a funnel like active site WD domain G beta repeatRibbon diagram of the C terminal WD40 domain of Tup1 a transcriptional co repressor in yeast which adopts a 7 bladed beta propeller fold Ribbon is colored from blue N terminus to red C terminus PDB 1erj 1 IdentifiersSymbolWD40PfamPF00400Pfam clanCL0186InterProIPR001680PROSITEPDOC00574SCOP21gp2 SCOPe SUPFAMCDDcd00200Available protein structures Pfam structures ECOD PDBRCSB PDB PDBe PDBjPDBsumstructure summary Contents 1 Structure 2 Function 3 Clinical Significance 4 Examples 4 1 Domains 5 References 6 Further reading 7 External linksStructure editEach beta sheet typically has four anti parallel b strands arranged in the beta zigzag motif 2 The strands are twisted so that the first and fourth strands are almost perpendicular to each other 3 There are five classes of beta propellers each arrangement being a highly symmetrical structure with 4 8 beta sheets all of which generally form a central tunnel that yields pseudo symmetric axes 2 While the protein s official active site for ligand binding is formed at one end of the central tunnel by loops between individual beta strands protein protein interactions can occur at multiple areas around the domain Depending on the packing and tilt of the beta sheets and beta strands the beta propeller may have a central pocket in place of a tunnel 4 The beta propeller structure is stabilized mainly through hydrophobic interactions of the beta sheets while additional stability may come from hydrogen bonds formed between the beta sheets of the C and N terminal ends In effect this closes the circle which can occur even more strongly in 4 bladed proteins via a disulfide bond 2 The chaperones Hsp70 and CCT have been shown to sequentially bind nascent beta propellers as they emerge from the ribosome These chaperones prevent non native inter blade interactions from forming until the entire beta propeller is synthesized 5 Many beta propellers are dependent on CCT for expression 6 7 8 In at least one case ions have been shown to increase stability by binding deep in the central tunnel of the beta propeller 4 Murzin proposed a geometric model to describe the structural principles of the beta propeller 9 According to this model the seven bladed propeller was the most favored arrangement in geometric terms Despite its highly conserved nature beta propellers are well known for their plasticity Beyond having a variety of allowed beta sheets per domain it can also accommodate other domains into its beta sheets Additionally there are proteins that have shown variance in the number of beta strands per beta sheet Rather than having the typical four beta strands in a sheet beta lactamase inhibitor protein II only has three beta strands per sheet while the phytase of Bacillus subtilis has five beta strands per beta sheet 2 Function editDue to its structure and plasticity protein protein interactions can form with the top bottom central channel and side faces of the beta propeller 4 The function of the propeller can vary based on the blade number Four bladed beta propellers function mainly as transport proteins and because of its structure they have a conformation that is favorable for substrate binding 4 Unlike larger beta propellers four bladed beta propellers usually cannot perform catalysis themselves but act instead to aid in catalysis by performing the aforementioned functions Five bladed propellers can act as transferases hydrolases and sugar binding proteins 4 Six and seven bladed propellers perform a much broader variety of functions in comparison to four and five bladed propellers These functions can include acting as ligand binding proteins hydrolases lyases isomerases signaling proteins structural proteins and oxidoreductases 4 Variations in the larger five to eight bladed beta propellers can allow for even more specific functions This is the case with the C terminal region of GyrA which expresses a positively charged surface ideal for binding DNA Two alpha helices coming out of the six bladed beta propeller of serum paraoxonase may provide a hydrophobic region ideal for anchoring membranes DNA damage binding protein 1 has three beta propellers in which the connection between two of the propellers is inserted into the third propeller potentially allowing for its unique function 4 Clinical Significance editBeta propeller protein associated neurodegeneration BPAN is a condition characterized by early onset seizures developmental delays and intellectual disability With aging muscle and cognitive degeneration may also occur Variants of the WDR45 gene have been identified in both males and females with this condition 10 Familial hypercholesterolemia is a human genetic disease caused by mutations to the gene that encodes low density lipoprotein receptor LDLR a protein which has at least one beta propeller This disease causes increased concentrations of low density lipoprotein LDL and cholesterol which can lead to further consequences such as coronary atherosclerosis Confirmed mutations have been shown to interfere with hydrogen bonding between blades of the beta propeller 2 The beta propeller has been used in protein engineering in several cases Yoshida et al for example worked with glucose dehydrogenase GDH having a six blade beta propeller to make an enzyme ideal for use as a glucose sensor They succeeded in engineering a GDH chimera which had a higher thermostability higher co factor binding stability and increased substrate specificity These properties were attributed to increased hydrophobic interactions due to mutations at the C terminus of the beta propeller 2 The beta propeller domain of the influenza virus neuraminidase are often used for drug design Through study of this enzyme researchers have developed influenza neuraminidase inhibitors which effectively block the influenza neuraminidase and consequently slowing or stopping the progression of the influenza infection 2 Examples editThe influenza virus protein viral neuraminidase is a six bladed beta propeller protein whose active form is a tetramer 11 It is one of two proteins present in the viral envelope and catalyzes the cleavage of sialic acid moieties from cell membrane proteins to aid in the targeting of newly produced virions to previously uninfected cells 12 WD40 repeats also known as beta transducin repeats are short fragments found primarily in eukaryotes 13 14 They usually form beta propellers with 7 8 blades but have also been shown to form structural domains with 4 to 16 repeated units critical for protein protein interactions WD40 protein motifs are involved in a variety of functions including signal transduction transcription regulation and regulation of the cell cycle They also work as sites for protein protein interactions and can even play a role in the assembly of protein complexes Specificity of these structural domains are determined by the sequence of the protein outside of itself 15 A beta propeller is a critical component of LDLR and aids in a pH based conformational change At neutral pH the LDLR is in an extended linear conformation and can bind ligands PCSK9 At acidic pH the linear conformation changes to a hairpin structure such that ligand binding sites bind to the beta propeller preventing ligand binding 16 17 Beta propeller phytases consist of a six bladed b propeller structure Phytases are phosphatases that can hydrolyze the ester bonds of phytate the major form of phosphate storage in plants Through this process phosphate that is normally inaccessible to livestock becomes available Most livestock feed has added inorganic phosphate which when excreted can cause environmental pollution The addition of phytase instead of phosphate into livestock feed would allow for animals to break down the phosphate already available in the plant matter This would theoretically produce less pollution as less of the excess phosphate would be excreted 18 Domains edit Repeat domains known to fold into a beta propeller include WD40 YWTD Kelch YVTN RIVW PD40 and many more Their sequences tend to group together suggesting a close evolutionary link They are also related to many beta containing domains 19 References edit Sprague ER Redd MJ Johnson AD Wolberger C June 2000 Structure of the C terminal domain of Tup1 a corepressor of transcription in yeast The EMBO Journal 19 12 3016 27 doi 10 1093 emboj 19 12 3016 PMC 203344 PMID 10856245 a b c d e f g Beta propellers Associated Functions and their Role in Human Diseases ResearchGate Retrieved 2018 11 17 Kuriyan Konforti Wemmer John Boyana David 2013 The molecules of life physical and chemical principles New York Garland Science pp 163 164 ISBN 9780815341888 a href Template Cite book html title Template Cite book cite book a CS1 maint multiple names authors list link a b c d e f g Chen CK Chan NL Wang AH October 2011 The many blades of the b propeller proteins conserved but versatile Trends in Biochemical Sciences 36 10 553 61 doi 10 1016 j tibs 2011 07 004 PMID 21924917 Stein KC Kriel A Frydman J July 2019 Nascent Polypeptide Domain Topology and Elongation Rate Direct the Cotranslational Hierarchy of Hsp70 and TRiC CCT Molecular Cell 75 6 1117 1130 e5 doi 10 1016 j molcel 2019 06 036 PMC 6953483 PMID 31400849 Plimpton RL Cuellar J Lai CW Aoba T Makaju A Franklin S et al February 2015 Structures of the Gb CCT and PhLP1 Gb CCT complexes reveal a mechanism for G protein b subunit folding and Gbg dimer assembly Proceedings of the National Academy of Sciences of the United States of America 112 8 2413 8 Bibcode 2015PNAS 112 2413P doi 10 1073 pnas 1419595112 PMC 4345582 PMID 25675501 Cuellar J Ludlam WG Tensmeyer NC Aoba T Dhavale M Santiago C et al June 2019 Structural and functional analysis of the role of the chaperonin CCT in mTOR complex assembly Nature Communications 10 1 2865 Bibcode 2019NatCo 10 2865C doi 10 1038 s41467 019 10781 1 PMC 6599039 PMID 31253771 Ludlam WG Aoba T Cuellar J Bueno Carrasco MT Makaju A Moody JD Franklin S Valpuesta JM Willardson BM 2019 11 01 Molecular architecture of the Bardet Biedl syndrome protein 2 7 9 subcomplex The Journal of Biological Chemistry 294 44 16385 16399 doi 10 1074 jbc RA119 010150 hdl 10261 240872 PMC 6827290 PMID 31530639 Murzin AG October 1992 Structural principles for the propeller assembly of beta sheets the preference for seven fold symmetry Proteins 14 2 191 201 doi 10 1002 prot 340140206 PMID 1409568 S2CID 22228091 Gregory A Kurian MA Haack T Hayflick SJ Hogarth P 1993 Adam MP Ardinger HH Pagon RA Wallace SE eds Beta Propeller Protein Associated Neurodegeneration University of Washington Seattle PMID 28211668 Retrieved 2018 11 20 a href Template Cite book html title Template Cite book cite book a work ignored help Air GM July 2012 Influenza neuraminidase Influenza and Other Respiratory Viruses 6 4 245 56 doi 10 1111 j 1750 2659 2011 00304 x PMC 3290697 PMID 22085243 Matrosovich MN Matrosovich TY Gray T Roberts NA Klenk HD November 2004 Neuraminidase is important for the initiation of influenza virus infection in human airway epithelium Journal of Virology 78 22 12665 7 doi 10 1128 JVI 78 22 12665 12667 2004 PMC 525087 PMID 15507653 Neer EJ Schmidt CJ Nambudripad R Smith TF September 1994 The ancient regulatory protein family of WD repeat proteins Nature 371 6495 297 300 Bibcode 1994Natur 371 297N doi 10 1038 371297a0 PMID 8090199 S2CID 600856 Smith TF Gaitatzes C Saxena K Neer EJ May 1999 The WD repeat a common architecture for diverse functions Trends in Biochemical Sciences 24 5 181 5 doi 10 1016 S0968 0004 99 01384 5 PMID 10322433 EMBL EBI InterPro WD40 like Beta Propeller IPR011659 lt InterPro lt EMBL EBI www ebi ac uk Retrieved 2018 11 19 Zhang DW Garuti R Tang WJ Cohen JC Hobbs HH September 2008 Structural requirements for PCSK9 mediated degradation of the low density lipoprotein receptor Proceedings of the National Academy of Sciences of the United States of America 105 35 13045 50 Bibcode 2008PNAS 10513045Z doi 10 1073 pnas 0806312105 PMC 2526098 PMID 18753623 Betteridge DJ February 2013 Cardiovascular endocrinology in 2012 PCSK9 an exciting target for reducing LDL cholesterol levels Nature Reviews Endocrinology 9 2 76 8 doi 10 1038 nrendo 2012 254 PMID 23296165 S2CID 27839784 Chen CC Cheng KJ Ko TP Guo RT 2015 01 09 Current Progresses in Phytase Research Three Dimensional Structure and Protein Engineering ChemBioEng Reviews 2 2 76 86 doi 10 1002 cben 201400026 Kopec KO Lupas AN 2013 b Propeller blades as ancestral peptides in protein evolution PLOS ONE 8 10 e77074 Bibcode 2013PLoSO 877074K doi 10 1371 journal pone 0077074 PMC 3797127 PMID 24143202 Further reading editBranden C Tooze J 1999 Introduction to Protein Structure 2nd ed Garland Publishing New York NY External links editSCOP 4 bladed beta propellers Archived 2016 03 04 at the Wayback Machine SCOP 5 bladed beta propellers Archived 2016 03 04 at the Wayback Machine SCOP 6 bladed beta propellers Archived 2017 03 24 at the Wayback Machine SCOP 7 bladed beta propellers Archived 2017 03 24 at the Wayback Machine SCOP 8 bladed beta propellers Archived 2016 03 04 at the Wayback Machine Retrieved from https en wikipedia org w index php title Beta propeller amp oldid 1171079828, wikipedia, wiki, book, books, library,

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