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EF hand

January 01, 1970

The EF hand is a helix–loop–helix structural domain or motif found in a large family of calcium-binding proteins.

EF hand
Structure of the recombinant Paramecium tetraurelia calmodulin.[1]
Identifiers
Symbolefhand
PfamPF00036
InterProIPR002048
PROSITEPDOC00018
SCOP21osa / SCOPe / SUPFAM
CDDcd00051
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

The EF-hand motif contains a helix–loop–helix topology, much like the spread thumb and forefinger of the human hand, in which the Ca2+ ions are coordinated by ligands within the loop. The motif takes its name from traditional nomenclature used in describing the protein parvalbumin, which contains three such motifs and is probably involved in muscle relaxation via its calcium-binding activity.

The EF-hand consists of two alpha helices linked by a short loop region (usually about 12 amino acids) that usually binds calcium ions. EF-hands also appear in each structural domain of the signaling protein calmodulin and in the muscle protein troponin-C.

Calcium ion binding site edit

 
EF-hand Ca2+ binding motif.

The calcium ion is coordinated in a pentagonal bipyramidal configuration. The six residues involved in the binding are in positions 1, 3, 5, 7, 9 and 12; these residues are denoted by X, Y, Z, -Y, -X and -Z. The invariant Glu or Asp at position 12 provides two oxygens for liganding calcium (bidentate ligand).

The calcium ion is bound by both protein backbone atoms and by amino acid side chains, specifically those of the anionic amino acid residues aspartate and glutamate. These residues are negatively charged and will make a charge-interaction with the positively charged calcium ion. The EF hand motif was among the first structural motifs whose sequence requirements were analyzed in detail. Five of the loop residues bind calcium and thus have a strong preference for oxygen-containing side chains, especially aspartate and glutamate. The sixth residue in the loop is necessarily glycine due to the conformational requirements of the backbone. The remaining residues are typically hydrophobic and form a hydrophobic core that binds and stabilizes the two helices.

Upon binding to Ca2+, this motif may undergo conformational changes that enable Ca2+-regulated functions as seen in Ca2+ effectors such as calmodulin (CaM) and troponin C (TnC) and Ca2+ buffers such as calreticulin and calbindin D9k. While the majority of the known EF-hand calcium-binding proteins (CaBPs) contain paired EF-hand motifs, CaBPs with single EF hands have also been discovered in both bacteria and eukaryotes. In addition, "EF-hand-like motifs" have been found in a number of bacteria. Although the coordination properties remain similar with the canonical 29-residue helix–loop–helix EF-hand motif, the EF-hand-like motifs differ from EF-hands in that they contain deviations in the secondary structure of the flanking sequences and/or variation in the length of the Ca2+-coordinating loop.

EF hands have very high selectivity for calcium. For example, the dissociation constant of alpha parvalbumin for Ca2+ is ~1000 times lower than that for the similar ion Mg2+.[2] This high selectivity is due to the relatively rigid coordination geometry, the presence of multiple charged amino acid side chains in the binding site, as well as the ion solvation properties.[3][4][5]

Prediction edit

 
Summary of motif signatures used for prediction of EF-hands.

Pattern (motif signature) search is one of the most straightforward ways to predict continuous EF-hand Ca2+-binding sites in proteins. Based on the sequence alignment results of canonical EF-hand motifs, especially the conserved side chains directly involved in Ca2+ binding, a pattern PS50222 has been generated to predict canonical EF-hand sites. Prediction servers may be found in the external links section.

Classification edit

Since the delineation of the EF-hand motif in 1973, the family of EF-hand proteins has expanded to include at least 66 subfamilies thus far. EF-hand motifs are divided into two major structural groups:

  • Canonical EF-hands as seen in calmodulin (CaM) and the prokaryotic CaM-like protein calerythrin. The 12-residue canonical EF-hand loop binds Ca2+ mainly via sidechain carboxylates or carbonyls (loop sequence positions 1, 3, 5, 12). The residue at the –X axis coordinates the Ca2+ ion through a bridged water molecule. The EF-hand loop has a bidentate ligand (Glu or Asp) at axis –Z.
  • Pseudo EF-hands exclusively found in the N-termini of S100 and S100-like proteins. The 14-residue pseudo EF-hand loop chelates Ca2+ primarily via backbone carbonyls (positions 1, 4, 6, 9).
 
Phylogenetic tree of the EF-hand protein family.

Additional points:

  • EF-hand-like proteins with diversified flanking structural elements around the Ca2+-binding loop have been reported in bacteria and viruses. These prokaryotic EF-hand-like proteins are widely implicated in Ca2+ signaling and homeostasis in bacteria. They contain flexible lengths of Ca2+-binding loops that differ from the EF-hand motifs. However, their coordination properties resemble classical EF-hand motifs.
    • For example, the semi-continuous Ca2+-binding site in D-galactose-binding protein (GBP) contains a nine-residue loop. The Ca2+ ion is coordinated by seven protein oxygen atoms, five of which are from the loop mimicking the canonical EF-loop whereas the other two are from the carboxylate group of a distant Glu.
    • Another example is a novel domain named Excalibur (extracellular Ca2+-binding region) isolated from Bacillus subtilis. This domain has a conserved 10-residue Ca2+-binding loop strikingly similar to the canonical 12-residue EF-hand loop.
    • The diversity of the structure of the flanking region is illustrated by the discovery of EF-hand-like domains in bacterial proteins. For example, a helix–loop–strand instead of the helix–loop–helix structure is in periplasmic galactose-binding protein (Salmonella typhimurium, PDB: 1gcg​) or alginate-binding protein (Sphingomonas sp., 1kwh​); the entering helix is missing in protective antigen (Bacillus anthracis, 1acc​) or dockerin (Clostridium thermocellum, 1daq​).

Among all the structures reported to date, the majority of EF-hand motifs are paired either between two canonical or one pseudo and one canonical motifs. For proteins with odd numbers of EF-hands, such as the penta-EF-hand calpain, EF-hand motifs were coupled through homo- or hetero-dimerization. The recently-identified EF-hand containing ER Ca2+ sensor protein, stromal interaction molecule 1 and 2 (STIM1, STIM2), has been shown to contain a Ca2+-binding canonical EF-hand motif that pairs with an immediate, downstream atypical "hidden" non-Ca2+-binding EF-hand. Single EF-hand motifs can serve as protein-docking modules: for example, the single EF hand in the NKD1 and NKD2 proteins binds the Dishevelled (DVL1, DVL2, DVL3) proteins.

Functionally, the EF-hands can be divided into two classes:

  1. signaling proteins
  2. buffering/transport proteins.

The first group is the largest and includes the most well-known members of the family such as calmodulin, troponin C and S100B. These proteins typically undergo a calcium-dependent conformational change which opens a target binding site. The latter group is represented by calbindin D9k and these proteins do not undergo calcium dependent conformational changes.

Subfamilies edit

  • EPS15 homology (EH) domain – InterPro: IPR000261

Examples edit

Aequorin edit

Aequorin is a calcium binding protein (CaBP) isolated from the cnidarian Aequorea victoria. Aequorin belongs to the EF-hand family of CaBPs, with EF-hand loops that are closely related to CaBPs in mammals. In addition, aequorin has been used for years as an indicator of Ca2+ and has been shown to be safe and well tolerated by cells. Aequorin is made up of two components – the calcium binding component apoaequorin (AQ) and the chemiluminescent molecule coelenterazine. The AQ portion of this protein contains the EF-hand calcium binding domains.[6]

Human proteins edit

Humans proteins containing this domain include:

See also edit

  • Another distinct calcium-binding motif composed of alpha helices is the dockerin domain.

References edit

  1. ^ Ban C, Ramakrishnan B, Ling KY, Kung C, Sundaralingam M (January 1994). "Structure of the recombinant Paramecium tetraurelia calmodulin at 1.68 A resolution". Acta Crystallogr. D. 50 (Pt 1): 50–63. doi:10.1107/S0907444993007991. PMID 15299476.
  2. ^ Schwaller, B. (13 October 2010). "Cytosolic Ca2+ Buffers". Cold Spring Harbor Perspectives in Biology. 2 (11): a004051. doi:10.1101/cshperspect.a004051. PMC 2964180. PMID 20943758.
  3. ^ Gifford, Jessica L.; Walsh, Michael P.; Vogel, Hans J. (15 July 2007). "Structures and metal-ion-binding properties of the Ca -binding helix–loop–helix EF-hand motifs". Biochemical Journal. 405 (2): 199–221. doi:10.1042/BJ20070255. PMID 17590154.
  4. ^ Dudev, Todor; Lim, Carmay (16 September 2013). "Competition among Metal Ions for Protein Binding Sites: Determinants of Metal Ion Selectivity in Proteins". Chemical Reviews. 114 (1): 538–556. doi:10.1021/cr4004665. PMID 24040963.
  5. ^ Jing, Zhifeng; Liu, Chengwen; Qi, Rui; Ren, Pengyu (23 July 2018). "Many-body effect determines the selectivity for Ca and Mg in proteins". Proceedings of the National Academy of Sciences. 115 (32): E7495–E7501. doi:10.1073/pnas.1805049115. PMC 6094099. PMID 30038003.
  6. ^ Detert JA, Adams EL, Lescher JD, Lyons JA, Moyer JR (2013). "Pretreatment with Apoaequorin Protects Hippocampal CA1 Neurons from Oxygen-Glucose Deprivation". PLOS ONE. 8 (11): e79002. doi:10.1371/journal.pone.0079002. PMC 3823939. PMID 24244400.

Further reading edit

  • Branden C, Tooze J (1999). "Chapter 2: Motifs of protein structure". Introduction to Protein Structure. New York: Garland Pub. pp. 24–25. ISBN 0-8153-2305-0.
  • Nakayama S, Kretsinger RH (1994). "Evolution of the EF-hand family of proteins". Annu Rev Biophys Biomol Struct. 23: 473–507. doi:10.1146/annurev.bb.23.060194.002353. PMID 7919790.
  • Zhou Y, Yang W, Kirberger M, Lee HW, Ayalasomayajula G, Yang JJ (November 2006). "Prediction of EF-hand calcium-binding proteins and analysis of bacterial EF-hand proteins". Proteins. 65 (3): 643–55. doi:10.1002/prot.21139. PMID 16981205. S2CID 8904181.
  • Zhou Y, Frey TK, Yang JJ (July 2009). "Viral calciomics: interplays between Ca2+ and virus". Cell Calcium. 46 (1): 1–17. doi:10.1016/j.ceca.2009.05.005. PMC 3449087. PMID 19535138.
  • Nakayama S, Moncrief ND, Kretsinger RH (May 1992). "Evolution of EF-hand calcium-modulated proteins. II. Domains of several subfamilies have diverse evolutionary histories". J. Mol. Evol. 34 (5): 416–48. doi:10.1007/BF00162998. PMID 1602495. S2CID 34614223.
  • Hogue CW, MacManus JP, Banville D, Szabo AG (July 1992). "Comparison of terbium (III) luminescence enhancement in mutants of EF hand calcium binding proteins". J. Biol. Chem. 267 (19): 13340–7. doi:10.1016/S0021-9258(18)42216-8. PMID 1618836.
  • Bairoch A, Cox JA (September 1990). "EF-hand motifs in inositol phospholipid-specific phospholipase C". FEBS Lett. 269 (2): 454–6. doi:10.1016/0014-5793(90)81214-9. PMID 2401372.
  • Finn BE, Forsén S (January 1995). "The evolving model of calmodulin structure, function and activation". Structure. 3 (1): 7–11. doi:10.1016/S0969-2126(01)00130-7. PMID 7743133.
  • Stathopulos PB, Zheng L, Li GY, Plevin MJ, Ikura M (October 2008). "Structural and mechanistic insights into STIM1-mediated initiation of store-operated calcium entry". Cell. 135 (1): 110–22. doi:10.1016/j.cell.2008.08.006. PMID 18854159.
  • Nelson MR, Thulin E, Fagan PA, Forsén S, Chazin WJ (February 2002). "The EF-hand domain: a globally cooperative structural unit". Protein Sci. 11 (2): 198–205. doi:10.1110/ps.33302. PMC 2373453. PMID 11790829.

External links edit

January 01, 1970
hand, helix, loop, helix, structural, domain, motif, found, large, family, calcium, binding, proteins, structure, recombinant, paramecium, tetraurelia, calmodulin, identifierssymbolefhandpfampf00036interproipr002048prositepdoc00018scop21osa, scope, supfamcddcd. The EF hand is a helix loop helix structural domain or motif found in a large family of calcium binding proteins EF handStructure of the recombinant Paramecium tetraurelia calmodulin 1 IdentifiersSymbolefhandPfamPF00036InterProIPR002048PROSITEPDOC00018SCOP21osa SCOPe SUPFAMCDDcd00051Available protein structures Pfam structures ECOD PDBRCSB PDB PDBe PDBjPDBsumstructure summary The EF hand motif contains a helix loop helix topology much like the spread thumb and forefinger of the human hand in which the Ca2 ions are coordinated by ligands within the loop The motif takes its name from traditional nomenclature used in describing the protein parvalbumin which contains three such motifs and is probably involved in muscle relaxation via its calcium binding activity The EF hand consists of two alpha helices linked by a short loop region usually about 12 amino acids that usually binds calcium ions EF hands also appear in each structural domain of the signaling protein calmodulin and in the muscle protein troponin C Contents 1 Calcium ion binding site 2 Prediction 3 Classification 3 1 Subfamilies 4 Examples 4 1 Aequorin 4 2 Human proteins 5 See also 6 References 7 Further reading 8 External linksCalcium ion binding site edit nbsp EF hand Ca2 binding motif The calcium ion is coordinated in a pentagonal bipyramidal configuration The six residues involved in the binding are in positions 1 3 5 7 9 and 12 these residues are denoted by X Y Z Y X and Z The invariant Glu or Asp at position 12 provides two oxygens for liganding calcium bidentate ligand The calcium ion is bound by both protein backbone atoms and by amino acid side chains specifically those of the anionic amino acid residues aspartate and glutamate These residues are negatively charged and will make a charge interaction with the positively charged calcium ion The EF hand motif was among the first structural motifs whose sequence requirements were analyzed in detail Five of the loop residues bind calcium and thus have a strong preference for oxygen containing side chains especially aspartate and glutamate The sixth residue in the loop is necessarily glycine due to the conformational requirements of the backbone The remaining residues are typically hydrophobic and form a hydrophobic core that binds and stabilizes the two helices Upon binding to Ca2 this motif may undergo conformational changes that enable Ca2 regulated functions as seen in Ca2 effectors such as calmodulin CaM and troponin C TnC and Ca2 buffers such as calreticulin and calbindin D9k While the majority of the known EF hand calcium binding proteins CaBPs contain paired EF hand motifs CaBPs with single EF hands have also been discovered in both bacteria and eukaryotes In addition EF hand like motifs have been found in a number of bacteria Although the coordination properties remain similar with the canonical 29 residue helix loop helix EF hand motif the EF hand like motifs differ from EF hands in that they contain deviations in the secondary structure of the flanking sequences and or variation in the length of the Ca2 coordinating loop EF hands have very high selectivity for calcium For example the dissociation constant of alpha parvalbumin for Ca2 is 1000 times lower than that for the similar ion Mg2 2 This high selectivity is due to the relatively rigid coordination geometry the presence of multiple charged amino acid side chains in the binding site as well as the ion solvation properties 3 4 5 Prediction edit nbsp Summary of motif signatures used for prediction of EF hands Pattern motif signature search is one of the most straightforward ways to predict continuous EF hand Ca2 binding sites in proteins Based on the sequence alignment results of canonical EF hand motifs especially the conserved side chains directly involved in Ca2 binding a pattern PS50222 has been generated to predict canonical EF hand sites Prediction servers may be found in the external links section Classification editSince the delineation of the EF hand motif in 1973 the family of EF hand proteins has expanded to include at least 66 subfamilies thus far EF hand motifs are divided into two major structural groups Canonical EF hands as seen in calmodulin CaM and the prokaryotic CaM like protein calerythrin The 12 residue canonical EF hand loop binds Ca2 mainly via sidechain carboxylates or carbonyls loop sequence positions 1 3 5 12 The residue at the X axis coordinates the Ca2 ion through a bridged water molecule The EF hand loop has a bidentate ligand Glu or Asp at axis Z Pseudo EF hands exclusively found in the N termini of S100 and S100 like proteins The 14 residue pseudo EF hand loop chelates Ca2 primarily via backbone carbonyls positions 1 4 6 9 nbsp Phylogenetic tree of the EF hand protein family Additional points EF hand like proteins with diversified flanking structural elements around the Ca2 binding loop have been reported in bacteria and viruses These prokaryotic EF hand like proteins are widely implicated in Ca2 signaling and homeostasis in bacteria They contain flexible lengths of Ca2 binding loops that differ from the EF hand motifs However their coordination properties resemble classical EF hand motifs For example the semi continuous Ca2 binding site in D galactose binding protein GBP contains a nine residue loop The Ca2 ion is coordinated by seven protein oxygen atoms five of which are from the loop mimicking the canonical EF loop whereas the other two are from the carboxylate group of a distant Glu Another example is a novel domain named Excalibur extracellular Ca2 binding region isolated from Bacillus subtilis This domain has a conserved 10 residue Ca2 binding loop strikingly similar to the canonical 12 residue EF hand loop The diversity of the structure of the flanking region is illustrated by the discovery of EF hand like domains in bacterial proteins For example a helix loop strand instead of the helix loop helix structure is in periplasmic galactose binding protein Salmonella typhimurium PDB 1gcg or alginate binding protein Sphingomonas sp 1kwh the entering helix is missing in protective antigen Bacillus anthracis 1acc or dockerin Clostridium thermocellum 1daq Among all the structures reported to date the majority of EF hand motifs are paired either between two canonical or one pseudo and one canonical motifs For proteins with odd numbers of EF hands such as the penta EF hand calpain EF hand motifs were coupled through homo or hetero dimerization The recently identified EF hand containing ER Ca2 sensor protein stromal interaction molecule 1 and 2 STIM1 STIM2 has been shown to contain a Ca2 binding canonical EF hand motif that pairs with an immediate downstream atypical hidden non Ca2 binding EF hand Single EF hand motifs can serve as protein docking modules for example the single EF hand in the NKD1 and NKD2 proteins binds the Dishevelled DVL1 DVL2 DVL3 proteins Functionally the EF hands can be divided into two classes signaling proteins buffering transport proteins The first group is the largest and includes the most well known members of the family such as calmodulin troponin C and S100B These proteins typically undergo a calcium dependent conformational change which opens a target binding site The latter group is represented by calbindin D9k and these proteins do not undergo calcium dependent conformational changes Subfamilies edit EPS15 homology EH domain InterPro IPR000261Examples editAequorin edit Aequorin is a calcium binding protein CaBP isolated from the cnidarian Aequorea victoria Aequorin belongs to the EF hand family of CaBPs with EF hand loops that are closely related to CaBPs in mammals In addition aequorin has been used for years as an indicator of Ca2 and has been shown to be safe and well tolerated by cells Aequorin is made up of two components the calcium binding component apoaequorin AQ and the chemiluminescent molecule coelenterazine The AQ portion of this protein contains the EF hand calcium binding domains 6 Human proteins edit Humans proteins containing this domain include ACTN1 ACTN2 ACTN3 ACTN4 APBA2BP AYTL1 AYTL2 C14orf143 CABP1 CABP2 CABP3 CABP4 CABP5 CABP7 CALB1 CALB2 CALM2 CALM3 CALML3 CALML4 CALML5 CALML6 CALN1 CALU CAPN1 CAPN11 CAPN2 CAPN3 CAPN9 CAPNS1 CAPNS2 CAPS CAPS2 CAPSL CBARA1 CETN1 CETN2 CETN3 CHP CHP2 CIB1 CIB2 CIB3 CIB4 CRNN DGKA DGKB DGKG DST DUOX1 DUOX2 EFCAB1 EFCAB2 EFCAB4A EFCAB4B EFCAB6 EFCBP1 EFCBP2 EFHA1 EFHA2 EFHB EFHC1 EFHD1 EFHD2 EPS15 EPS15L1 FKBP10 FKBP14 FKBP7 FKBP9 FKBP9L FREQ FSTL1 FSTL5 GCA GPD2 GUCA1A GUCA1B GUCA1C hippocalcin HPCAL1 HPCAL4 HZGJ IFPS ITSN1 ITSN2 KCNIP1 KCNIP2 KCNIP3 KCNIP4 KIAA1799 LCP1 MACF1 MRLC2 MRLC3 MST133 MYL1 MYL2 MYL5 MYL6B MYL7 MYL9 MYLC2PL MYLPF NCALD NIN NKD1 NKD2 NLP NOX5 NUCB1 NUCB2 OCM PDCD6 PEF1 PKD2 PLCD1 PLCD4 PLCH1 PLCH2 PLS1 PLS3 PP1187 PPEF1 PPEF2 PPP3R1 PPP3R2 PRKCSH PVALB RAB11FIP3 RASEF RASGRP RASGRP1 RASGRP2 RASGRP3 RCN1 RCN2 RCN3 RCV1 RCVRN REPS1 RHBDL3 RHOT1 RHOT2 RPTN RYR2 RYR3 S100A1 S100A11 S100A12 S100A6 S100A8 S100A9 S100B S100G S100Z SCAMC 2 SCGN SCN5A SDF4 SLC25A12 SLC25A13 SLC25A23 SLC25A24 SLC25A25 SPATA21 SPTA1 SPTAN1 SRI TBC1D9 TBC1D9B TCHH TESC TNNC1 TNNC2 USP32 VSNL1 ZZEF1See also editAnother distinct calcium binding motif composed of alpha helices is the dockerin domain References edit Ban C Ramakrishnan B Ling KY Kung C Sundaralingam M January 1994 Structure of the recombinant Paramecium tetraurelia calmodulin at 1 68 A resolution Acta Crystallogr D 50 Pt 1 50 63 doi 10 1107 S0907444993007991 PMID 15299476 Schwaller B 13 October 2010 Cytosolic Ca2 Buffers Cold Spring Harbor Perspectives in Biology 2 11 a004051 doi 10 1101 cshperspect a004051 PMC 2964180 PMID 20943758 Gifford Jessica L Walsh Michael P Vogel Hans J 15 July 2007 Structures and metal ion binding properties of the Ca binding helix loop helix EF hand motifs Biochemical Journal 405 2 199 221 doi 10 1042 BJ20070255 PMID 17590154 Dudev Todor Lim Carmay 16 September 2013 Competition among Metal Ions for Protein Binding Sites Determinants of Metal Ion Selectivity in Proteins Chemical Reviews 114 1 538 556 doi 10 1021 cr4004665 PMID 24040963 Jing Zhifeng Liu Chengwen Qi Rui Ren Pengyu 23 July 2018 Many body effect determines the selectivity for Ca and Mg in proteins Proceedings of the National Academy of Sciences 115 32 E7495 E7501 doi 10 1073 pnas 1805049115 PMC 6094099 PMID 30038003 Detert JA Adams EL Lescher JD Lyons JA Moyer JR 2013 Pretreatment with Apoaequorin Protects Hippocampal CA1 Neurons from Oxygen Glucose Deprivation PLOS ONE 8 11 e79002 doi 10 1371 journal pone 0079002 PMC 3823939 PMID 24244400 Further reading editBranden C Tooze J 1999 Chapter 2 Motifs of protein structure Introduction to Protein Structure New York Garland Pub pp 24 25 ISBN 0 8153 2305 0 Nakayama S Kretsinger RH 1994 Evolution of the EF hand family of proteins Annu Rev Biophys Biomol Struct 23 473 507 doi 10 1146 annurev bb 23 060194 002353 PMID 7919790 Zhou Y Yang W Kirberger M Lee HW Ayalasomayajula G Yang JJ November 2006 Prediction of EF hand calcium binding proteins and analysis of bacterial EF hand proteins Proteins 65 3 643 55 doi 10 1002 prot 21139 PMID 16981205 S2CID 8904181 Zhou Y Frey TK Yang JJ July 2009 Viral calciomics interplays between Ca2 and virus Cell Calcium 46 1 1 17 doi 10 1016 j ceca 2009 05 005 PMC 3449087 PMID 19535138 Nakayama S Moncrief ND Kretsinger RH May 1992 Evolution of EF hand calcium modulated proteins II Domains of several subfamilies have diverse evolutionary histories J Mol Evol 34 5 416 48 doi 10 1007 BF00162998 PMID 1602495 S2CID 34614223 Hogue CW MacManus JP Banville D Szabo AG July 1992 Comparison of terbium III luminescence enhancement in mutants of EF hand calcium binding proteins J Biol Chem 267 19 13340 7 doi 10 1016 S0021 9258 18 42216 8 PMID 1618836 Bairoch A Cox JA September 1990 EF hand motifs in inositol phospholipid specific phospholipase C FEBS Lett 269 2 454 6 doi 10 1016 0014 5793 90 81214 9 PMID 2401372 Finn BE Forsen S January 1995 The evolving model of calmodulin structure function and activation Structure 3 1 7 11 doi 10 1016 S0969 2126 01 00130 7 PMID 7743133 Stathopulos PB Zheng L Li GY Plevin MJ Ikura M October 2008 Structural and mechanistic insights into STIM1 mediated initiation of store operated calcium entry Cell 135 1 110 22 doi 10 1016 j cell 2008 08 006 PMID 18854159 Nelson MR Thulin E Fagan PA Forsen S Chazin WJ February 2002 The EF hand domain a globally cooperative structural unit Protein Sci 11 2 198 205 doi 10 1110 ps 33302 PMC 2373453 PMID 11790829 External links editEukaryotic Linear Motif resource motif class LIG EH 1 Eukaryotic Linear Motif resource motif class LIG IQ Eukaryotic Linear Motif resource motif class DOC PP2B LxvP 1 Eukaryotic Linear Motif resource motif class LIG IQ Nelson M Chazin W EF Hand Calcium Binding Proteins Data Library Vanderbilt University Retrieved 2009 08 29 Haiech J EF hand protein database EF handome European Calcium Society and the Universite Libre de Bruxelles Retrieved 2009 08 29 upon request to haiech pharma u strasbg fr Yang J Calciomics Georgia State University Archived from the original on 2009 10 12 Retrieved 2009 08 29 prediction server for EF hand calcium binding proteins Retrieved from https en wikipedia org w index php title EF hand amp oldid 1092136194, wikipedia, wiki, book, books, library,

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