fbpx
Wikipedia

Cation channel superfamily

The transmembrane cation channel superfamily was defined in InterPro and Pfam as the family of tetrameric ion channels. These include the sodium, potassium,[1] calcium, ryanodine receptor, HCN, CNG, CatSper, and TRP channels. This large group of ion channels apparently includes families 1.A.1, 1.A.2, 1.A.3, and 1.A.4 of the TCDB transporter classification.

Ion channel (eukaryotic)
Potassium channel Kv1.2 (with beta2 auxiliary subunits), structure in a membrane-like environment. Calculated hydrocarbon boundaries of the lipid bilayer are indicated by red and blue dots.
Identifiers
SymbolIon_trans
PfamPF00520
InterProIPR005821
SCOP21bl8 / SCOPe / SUPFAM
TCDB1.A.1
OPM superfamily8
OPM protein2a79
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
PDB1qg9A:157-176 2a79B:225-409 1ho7A:378-397 1ho2A:378-397 1ujlA:570-611
Ion channel (bacterial)
Potassium channel KcsA. Calculated hydrocarbon boundaries of the lipid bilayer are indicated by red and blue dots.
Identifiers
SymbolIon_trans_2
PfamPF07885
InterProIPR013099
SCOP21bl8 / SCOPe / SUPFAM
OPM protein1r3j
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
PDB1lnqE:25-100 2a0lB:169-250 1orqC:169-250

1k4cC:34-116 1r3iC:34-116 2bocC:34-116 1j95C:34-116 1r3lC:34-116 1jvmB:34-116 1bl8C:34-116 2a9hD:34-116 1k4dC:34-116 1r3jC:34-116 1r3kC:34-116 2bobC:34-116

1p7bB:77-151

They are described as minimally having two transmembrane helices flanking a loop which determines the ion selectivity of the channel pore. Many eukaryotic channels have four additional transmembrane helices (TM) (Pfam PF00520), related to or vestigial of voltage gating. The proteins with only two transmembrane helices (Pfam PF07885) are most commonly found in bacteria. This also includes the 2-TM inward-rectifier potassium channels (Pfam PF01007) found primarily in eukaryotes. There are commonly additional regulatory domains which serve to regulate ion conduction and channel gating. The pores may also be homotetramers or heterotetramers; where heterotetramers may be encoded as distinct genes or as multiple pore domains within a single polypeptide. The HVCN1 and Putative tyrosine-protein phosphatase proteins do not contain an expected ion conduction pore domain, but rather have homology only to the voltage sensor domain of voltage gated ion channels.

Human channels with 6 TM helices Edit

Cation Edit

Transient receptor potential Edit

Canonical Edit
Melastatin Edit
Vanilloid Edit
Mucolipin Edit
Ankyrin Edit
TRPP Edit
  • PKD1L3;

Calcium Edit

Voltage-dependent Edit

Sperm Edit

Ryanodine receptor Edit

Potassium Edit

Voltage-gated potassium Edit

Delayed rectifier Edit
A-type potassium Edit
  • Kvα1.x - Shaker-related: Kv1.4 (KCNA4)
  • Kvα3.x - Shaw-related: Kv3.3 (KCNC3), Kv3.4 (KCNC4)
  • Kvα4.x - Shal-related: Kv4.1 (KCND1), Kv4.2 (KCND2), Kv4.3 (KCND3)
Outward-rectifying Edit
Inwardly-rectifying Edit
Slowly activating Edit
Modifier/silencer Edit

Calcium-activated Edit

BK Edit
  • KCa1.1 (BK, Slo1, Maxi-K, KCNMA1)
SK Edit
  • KCa2.x: KCa2.1 (KCNN1) - SK1, KCa2.2 (KCNN2) - SK2, KCa2.3 (KCNN3) - SK3
  • KCa3.x: KCa3.1 (KCNN4) - SK4
  • KCa4.x: KCa4.1 (KCNT1) - SLACK, KCa4.2 (KCNT2) - SLICK
IK Edit
Other subfamilies Edit

Inward-rectifier potassium Edit

Sodium Edit

Cyclic nucleotide-gated Edit

Proton Edit

Related proteins Edit

Human channels with 2 TM helices in each subunit Edit

Potassium Edit

Tandem pore domain potassium channel Edit

Non-human channels Edit

Two-pore Edit

Pore-only potassium Edit

Ligand-gated potassium Edit

Voltage-gated potassium Edit

Prokaryotic KCa Edit

Voltage and cyclic nucleotide gated potassium Edit

Sodium Edit

Non-selective Edit

Prokaryotic inward-rectifier potassium Edit

Engineered Edit

References Edit

  1. ^ Choe S (February 2002). "Potassium channel structures". Nature Reviews. Neuroscience. 3 (2): 115–21. doi:10.1038/nrn727. PMID 11836519. S2CID 825973.
  2. ^ Chen GQ, Cui C, Mayer ML, Gouaux E (December 1999). "Functional characterization of a potassium-selective prokaryotic glutamate receptor". Nature. 402 (6763): 817–21. Bibcode:1999Natur.402..817C. doi:10.1038/45568. PMID 10617203. S2CID 4391943.
  3. ^ Jiang Y, Lee A, Chen J, Ruta V, Cadene M, Chait BT, MacKinnon R (May 2003). "X-ray structure of a voltage-dependent K+ channel". Nature. 423 (6935): 33–41. Bibcode:2003Natur.423...33J. doi:10.1038/nature01580. PMID 12721618. S2CID 4347957.
  4. ^ Milkman R (April 1994). "An Escherichia coli homologue of eukaryotic potassium channel proteins". Proceedings of the National Academy of Sciences of the United States of America. 91 (9): 3510–4. Bibcode:1994PNAS...91.3510M. doi:10.1073/pnas.91.9.3510. PMC 43609. PMID 8170937.
  5. ^ Jiang Y, Pico A, Cadene M, Chait BT, MacKinnon R (March 2001). "Structure of the RCK domain from the E. coli K+ channel and demonstration of its presence in the human BK channel". Neuron. 29 (3): 593–601. doi:10.1016/s0896-6273(01)00236-7. PMID 11301020. S2CID 17880955.
  6. ^ Jiang Y, Lee A, Chen J, Cadene M, Chait BT, MacKinnon R (May 2002). "Crystal structure and mechanism of a calcium-gated potassium channel". Nature. 417 (6888): 515–22. Bibcode:2002Natur.417..515J. doi:10.1038/417515a. PMID 12037559. S2CID 205029269.
  7. ^ Smith FJ, Pau VP, Cingolani G, Rothberg BS (2013). "Structural basis of allosteric interactions among Ca2+-binding sites in a K+ channel RCK domain". Nature Communications. 4: 2621. Bibcode:2013NatCo...4.2621S. doi:10.1038/ncomms3621. PMID 24126388.
  8. ^ Ye S, Li Y, Chen L, Jiang Y (September 2006). "Crystal structures of a ligand-free MthK gating ring: insights into the ligand gating mechanism of K+ channels". Cell. 126 (6): 1161–73. doi:10.1016/j.cell.2006.08.029. PMID 16990139. S2CID 418563.
  9. ^ Dvir H, Valera E, Choe S (August 2010). "Structure of the MthK RCK in complex with cadmium". Journal of Structural Biology. 171 (2): 231–7. doi:10.1016/j.jsb.2010.03.020. PMC 2956275. PMID 20371380.
  10. ^ Smith FJ, Pau VP, Cingolani G, Rothberg BS (December 2012). "Crystal structure of a Ba(2+)-bound gating ring reveals elementary steps in RCK domain activation". Structure. 20 (12): 2038–47. doi:10.1016/j.str.2012.09.014. PMC 3518701. PMID 23085076.
  11. ^ Cao Y, Jin X, Huang H, Derebe MG, Levin EJ, Kabaleeswaran V, Pan Y, Punta M, Love J, Weng J, Quick M, Ye S, Kloss B, Bruni R, Martinez-Hackert E, Hendrickson WA, Rost B, Javitch JA, Rajashankar KR, Jiang Y, Zhou M (March 2011). "Crystal structure of a potassium ion transporter, TrkH". Nature. 471 (7338): 336–40. Bibcode:2011Natur.471..336C. doi:10.1038/nature09731. PMC 3077569. PMID 21317882.
  12. ^ Cao Y, Pan Y, Huang H, Jin X, Levin EJ, Kloss B, Zhou M (April 2013). "Gating of the TrkH ion channel by its associated RCK protein TrkA". Nature. 496 (7445): 317–22. Bibcode:2013Natur.496..317C. doi:10.1038/nature12056. PMC 3726529. PMID 23598339.
  13. ^ Vieira-Pires RS, Szollosi A, Morais-Cabral JH (April 2013). "The structure of the KtrAB potassium transporter". Nature. 496 (7445): 323–8. Bibcode:2013Natur.496..323V. doi:10.1038/nature12055. hdl:10216/110345. PMID 23598340. S2CID 205233489.
  14. ^ Kong C, Zeng W, Ye S, Chen L, Sauer DB, Lam Y, Derebe MG, Jiang Y (December 2012). "Distinct gating mechanisms revealed by the structures of a multi-ligand gated K(+) channel". eLife. 1: e00184. doi:10.7554/eLife.00184. PMC 3510474. PMID 23240087.
  15. ^ Deller MC, Johnson HA, Miller MD, Spraggon G, Elsliger MA, Wilson IA, Lesley SA (2015). "Crystal structure of a two-subunit TrkA octameric gating ring assembly". PLOS ONE. 10 (3): e0122512. Bibcode:2015PLoSO..1022512D. doi:10.1371/journal.pone.0122512. PMC 4380455. PMID 25826626.
  16. ^ Clayton GM, Altieri S, Heginbotham L, Unger VM, Morais-Cabral JH (February 2008). "Structure of the transmembrane regions of a bacterial cyclic nucleotide-regulated channel". Proceedings of the National Academy of Sciences of the United States of America. 105 (5): 1511–5. Bibcode:2008PNAS..105.1511C. doi:10.1073/pnas.0711533105. PMC 2234175. PMID 18216238.
  17. ^ Ren D, Navarro B, Xu H, Yue L, Shi Q, Clapham DE (December 2001). "A prokaryotic voltage-gated sodium channel". Science. 294 (5550): 2372–5. Bibcode:2001Sci...294.2372R. doi:10.1126/science.1065635. PMID 11743207. S2CID 5721075.
  18. ^ Payandeh J, Scheuer T, Zheng N, Catterall WA (July 2011). "The crystal structure of a voltage-gated sodium channel". Nature. 475 (7356): 353–8. doi:10.1038/nature10238. PMC 3266868. PMID 21743477.
  19. ^ Shaya D, Findeisen F, Abderemane-Ali F, Arrigoni C, Wong S, Nurva SR, Loussouarn G, Minor DL (January 2014). "Structure of a prokaryotic sodium channel pore reveals essential gating elements and an outer ion binding site common to eukaryotic channels". Journal of Molecular Biology. 426 (2): 467–83. Bibcode:2014BpJ...106..130A. doi:10.1016/j.jmb.2013.10.010. PMC 3947372. PMID 24120938.
  20. ^ Zhang X, Ren W, DeCaen P, Yan C, Tao X, Tang L, Wang J, Hasegawa K, Kumasaka T, He J, Wang J, Clapham DE, Yan N (May 2012). "Crystal structure of an orthologue of the NaChBac voltage-gated sodium channel". Nature. 486 (7401): 130–4. Bibcode:2012Natur.486..130Z. doi:10.1038/nature11054. PMC 3979295. PMID 22678295.
  21. ^ McCusker EC, Bagnéris C, Naylor CE, Cole AR, D'Avanzo N, Nichols CG, Wallace BA (2012). "Structure of a bacterial voltage-gated sodium channel pore reveals mechanisms of opening and closing". Nature Communications. 3: 1102. Bibcode:2012NatCo...3.1102M. doi:10.1038/ncomms2077. PMC 3493636. PMID 23033078.
  22. ^ Shi N, Ye S, Alam A, Chen L, Jiang Y (March 2006). "Atomic structure of a Na+- and K+-conducting channel". Nature. 440 (7083): 570–4. Bibcode:2006Natur.440..570S. doi:10.1038/nature04508. PMID 16467789. S2CID 4355500.
  23. ^ Durell SR, Guy HR (2001). "A family of putative Kir potassium channels in prokaryotes". BMC Evolutionary Biology. 1: 14. doi:10.1186/1471-2148-1-14. PMC 64639. PMID 11806753.
  24. ^ Derebe MG, Sauer DB, Zeng W, Alam A, Shi N, Jiang Y (January 2011). "Tuning the ion selectivity of tetrameric cation channels by changing the number of ion binding sites". Proceedings of the National Academy of Sciences of the United States of America. 108 (2): 598–602. Bibcode:2011PNAS..108..598D. doi:10.1073/pnas.1013636108. PMC 3021048. PMID 21187421.
  25. ^ Sauer DB, Zeng W, Raghunathan S, Jiang Y (October 2011). "Protein interactions central to stabilizing the K+ channel selectivity filter in a four-sited configuration for selective K+ permeation". Proceedings of the National Academy of Sciences of the United States of America. 108 (40): 16634–9. Bibcode:2011PNAS..10816634S. doi:10.1073/pnas.1111688108. PMC 3189067. PMID 21933962.

External links Edit

  • "Voltage-gated Ion Channels". IUPHAR Database of Receptors and Ion Channels. International Union of Basic and Clinical Pharmacology.
This article incorporates text from the public domain Pfam and InterPro: IPR005821

cation, channel, superfamily, also, voltage, gated, channel, transmembrane, cation, channel, superfamily, defined, interpro, pfam, family, tetrameric, channels, these, include, sodium, potassium, calcium, ryanodine, receptor, catsper, channels, this, large, gr. See also Voltage gated ion channel The transmembrane cation channel superfamily was defined in InterPro and Pfam as the family of tetrameric ion channels These include the sodium potassium 1 calcium ryanodine receptor HCN CNG CatSper and TRP channels This large group of ion channels apparently includes families 1 A 1 1 A 2 1 A 3 and 1 A 4 of the TCDB transporter classification Ion channel eukaryotic Potassium channel Kv1 2 with beta2 auxiliary subunits structure in a membrane like environment Calculated hydrocarbon boundaries of the lipid bilayer are indicated by red and blue dots IdentifiersSymbolIon transPfamPF00520InterProIPR005821SCOP21bl8 SCOPe SUPFAMTCDB1 A 1OPM superfamily8OPM protein2a79Available protein structures Pfam structures ECOD PDBRCSB PDB PDBe PDBjPDBsumstructure summaryPDB1qg9 A 157 176 2a79 B 225 409 1ho7 A 378 397 1ho2 A 378 397 1ujl A 570 611Ion channel bacterial Potassium channel KcsA Calculated hydrocarbon boundaries of the lipid bilayer are indicated by red and blue dots IdentifiersSymbolIon trans 2PfamPF07885InterProIPR013099SCOP21bl8 SCOPe SUPFAMOPM protein1r3jAvailable protein structures Pfam structures ECOD PDBRCSB PDB PDBe PDBjPDBsumstructure summaryPDB1lnq E 25 100 2a0l B 169 250 1orq C 169 250 1k4c C 34 116 1r3i C 34 116 2boc C 34 116 1j95 C 34 116 1r3l C 34 116 1jvm B 34 116 1bl8 C 34 116 2a9h D 34 116 1k4d C 34 116 1r3j C 34 116 1r3k C 34 116 2bob C 34 116 1p7b B 77 151They are described as minimally having two transmembrane helices flanking a loop which determines the ion selectivity of the channel pore Many eukaryotic channels have four additional transmembrane helices TM Pfam PF00520 related to or vestigial of voltage gating The proteins with only two transmembrane helices Pfam PF07885 are most commonly found in bacteria This also includes the 2 TM inward rectifier potassium channels Pfam PF01007 found primarily in eukaryotes There are commonly additional regulatory domains which serve to regulate ion conduction and channel gating The pores may also be homotetramers or heterotetramers where heterotetramers may be encoded as distinct genes or as multiple pore domains within a single polypeptide The HVCN1 and Putative tyrosine protein phosphatase proteins do not contain an expected ion conduction pore domain but rather have homology only to the voltage sensor domain of voltage gated ion channels Contents 1 Human channels with 6 TM helices 1 1 Cation 1 1 1 Transient receptor potential 1 1 1 1 Canonical 1 1 1 2 Melastatin 1 1 1 3 Vanilloid 1 1 1 4 Mucolipin 1 1 1 5 Ankyrin 1 1 1 6 TRPP 1 2 Calcium 1 2 1 Voltage dependent 1 2 2 Sperm 1 2 3 Ryanodine receptor 1 3 Potassium 1 3 1 Voltage gated potassium 1 3 1 1 Delayed rectifier 1 3 1 2 A type potassium 1 3 1 3 Outward rectifying 1 3 1 4 Inwardly rectifying 1 3 1 5 Slowly activating 1 3 1 6 Modifier silencer 1 3 2 Calcium activated 1 3 2 1 BK 1 3 2 2 SK 1 3 2 3 IK 1 3 2 4 Other subfamilies 1 3 3 Inward rectifier potassium 1 4 Sodium 1 5 Cyclic nucleotide gated 1 6 Proton 1 7 Related proteins 2 Human channels with 2 TM helices in each subunit 2 1 Potassium 2 1 1 Tandem pore domain potassium channel 3 Non human channels 3 1 Two pore 3 2 Pore only potassium 3 3 Ligand gated potassium 3 4 Voltage gated potassium 3 5 Prokaryotic KCa 3 6 Voltage and cyclic nucleotide gated potassium 3 7 Sodium 3 8 Non selective 3 9 Prokaryotic inward rectifier potassium 3 10 Engineered 4 References 5 External linksHuman channels with 6 TM helices EditCation Edit Transient receptor potential Edit Main article Transient receptor potential channel Canonical Edit Main article Canonical TRP channels TRPC1 TRPC3 TRPC4 TRPC5 TRPC6 TRPC7Melastatin Edit Main article Melastatin TRP channels TRPM1 TRPM2 TRPM3 TRPM4 TRPM5 TRPM6 TRPM7 TRPM8Vanilloid Edit Main article Vanilloid TRP channels TRPV1 TRPV2 TRPV3 TRPV4 TRPV5 TRPV6Mucolipin Edit Main article Mucolipin TRP channels MCOLN1 MCOLN2 MCOLN3 Ankyrin Edit Main article Ankyrin TRP channels TRPA1TRPP Edit Main article Transient Receptor Potential Polycystic PKD1L3 Calcium Edit Voltage dependent Edit Main article Voltage dependent calcium channels CACNA1A CACNA1B CACNA1C CACNA1D CACNA1E CACNA1F CACNA1G CACNA1H CACNA1I CACNA1SSperm Edit Main article Cation channels of sperm CATSPER1 CATSPER2 CATSPER3 CATSPER4Ryanodine receptor Edit Main article Ryanodine receptor RYR1 RYR2 RYR3Potassium Edit Voltage gated potassium Edit Main article Voltage gated potassium channels Delayed rectifier Edit Kva1 x Shaker related Kv1 1 KCNA1 Kv1 2 KCNA2 Kv1 3 KCNA3 Kv1 5 KCNA5 Kv1 6 KCNA6 Kv1 7 KCNA7 Kv1 8 KCNA10 Kva2 x Shab related Kv2 1 KCNB1 Kv2 2 KCNB2 Kva3 x Shaw related Kv3 1 KCNC1 Kv3 2 KCNC2 Kva7 x Kv7 1 KCNQ1 KvLQT1 Kv7 2 KCNQ2 Kv7 3 KCNQ3 Kv7 4 KCNQ4 Kv7 5 KCNQ5 Kva10 x Kv10 1 KCNH1 A type potassium Edit Kva1 x Shaker related Kv1 4 KCNA4 Kva3 x Shaw related Kv3 3 KCNC3 Kv3 4 KCNC4 Kva4 x Shal related Kv4 1 KCND1 Kv4 2 KCND2 Kv4 3 KCND3 Outward rectifying Edit Kva10 x Kv10 2 KCNH5 Inwardly rectifying Edit Kva11 x ether a go go potassium channels Kv11 1 KCNH2 hERG Kv11 2 KCNH6 Kv11 3 KCNH7 Slowly activating Edit Kva12 x Kv12 1 KCNH8 Kv12 2 KCNH3 Kv12 3 KCNH4 Modifier silencer Edit Kva5 x Kv5 1 KCNF1 Kva6 x Kv6 1 KCNG1 Kv6 2 KCNG2 Kv6 3 KCNG3 Kv6 4 KCNG4 Kva8 x Kv8 1 KCNV1 Kv8 2 KCNV2 Kva9 x Kv9 1 KCNS1 Kv9 2 KCNS2 Kv9 3 KCNS3 Calcium activated Edit Main article Calcium activated potassium channels BK Edit Main article BK channels KCa1 1 BK Slo1 Maxi K KCNMA1 SK Edit Main article SK channels KCa2 x KCa2 1 KCNN1 SK1 KCa2 2 KCNN2 SK2 KCa2 3 KCNN3 SK3 KCa3 x KCa3 1 KCNN4 SK4 KCa4 x KCa4 1 KCNT1 SLACK KCa4 2 KCNT2 SLICKIK Edit Main article IK channels KCa3 1 IKCa1 SK4 KCNN4 Other subfamilies Edit KCa5 1 Slo3 KCNU1 Inward rectifier potassium Edit Main article Inward rectifier potassium ion channel Sodium Edit NALCN SCN1A SCN2A SCN2A2 SCN3A SCN4A SCN5A SCN7A SCN8A SCN9A SCN10A SCN11A SLC9A10 SLC9A11Cyclic nucleotide gated Edit CNGA1 CNGA2 CNGA3 CNGA4 CNGB1 CNGB3 HCN1 HCN2 HCN3 HCN4 ITPR1 ITPR2 ITPR3Proton Edit HVCN1Related proteins Edit TPTE part of the larger Voltage sensitive phosphatase familyHuman channels with 2 TM helices in each subunit EditPotassium Edit Tandem pore domain potassium channel Edit Main article Tandem pore domain potassium channel KCNK1 KCNK2 KCNK3 KCNK4 KCNK5 KCNK6 KCNK7 KCNK9 KCNK10 KCNK12 KCNK13 KCNK15 KCNK16 KCNK17 KCNK18Non human channels EditTwo pore Edit Main article Two pore channels TPCN1 TPCN2Pore only potassium Edit Main article Pore only potassium channels KcsALigand gated potassium Edit GluR0 2 Voltage gated potassium Edit Main article Voltage gated potassium channels KvAP 3 Prokaryotic KCa Edit Main article Prokaryotic KCa channels Kch 4 5 MthK 6 7 8 9 10 TrkA TrkH 11 12 KtrAB 13 GsuK 14 TM1088 15 Voltage and cyclic nucleotide gated potassium Edit MlotiK1 16 Sodium Edit NaChBac 17 NaVAb 18 NaVAe1 19 NaVAp 20 NaVMm 21 Non selective Edit NaK 22 Prokaryotic inward rectifier potassium Edit Main article Inward rectifier potassium channels KirBac 23 Engineered Edit NaK2CNG 24 NaK2K 25 References Edit Choe S February 2002 Potassium channel structures Nature Reviews Neuroscience 3 2 115 21 doi 10 1038 nrn727 PMID 11836519 S2CID 825973 Chen GQ Cui C Mayer ML Gouaux E December 1999 Functional characterization of a potassium selective prokaryotic glutamate receptor Nature 402 6763 817 21 Bibcode 1999Natur 402 817C doi 10 1038 45568 PMID 10617203 S2CID 4391943 Jiang Y Lee A Chen J Ruta V Cadene M Chait BT MacKinnon R May 2003 X ray structure of a voltage dependent K channel Nature 423 6935 33 41 Bibcode 2003Natur 423 33J doi 10 1038 nature01580 PMID 12721618 S2CID 4347957 Milkman R April 1994 An Escherichia coli homologue of eukaryotic potassium channel proteins Proceedings of the National Academy of Sciences of the United States of America 91 9 3510 4 Bibcode 1994PNAS 91 3510M doi 10 1073 pnas 91 9 3510 PMC 43609 PMID 8170937 Jiang Y Pico A Cadene M Chait BT MacKinnon R March 2001 Structure of the RCK domain from the E coli K channel and demonstration of its presence in the human BK channel Neuron 29 3 593 601 doi 10 1016 s0896 6273 01 00236 7 PMID 11301020 S2CID 17880955 Jiang Y Lee A Chen J Cadene M Chait BT MacKinnon R May 2002 Crystal structure and mechanism of a calcium gated potassium channel Nature 417 6888 515 22 Bibcode 2002Natur 417 515J doi 10 1038 417515a PMID 12037559 S2CID 205029269 Smith FJ Pau VP Cingolani G Rothberg BS 2013 Structural basis of allosteric interactions among Ca2 binding sites in a K channel RCK domain Nature Communications 4 2621 Bibcode 2013NatCo 4 2621S doi 10 1038 ncomms3621 PMID 24126388 Ye S Li Y Chen L Jiang Y September 2006 Crystal structures of a ligand free MthK gating ring insights into the ligand gating mechanism of K channels Cell 126 6 1161 73 doi 10 1016 j cell 2006 08 029 PMID 16990139 S2CID 418563 Dvir H Valera E Choe S August 2010 Structure of the MthK RCK in complex with cadmium Journal of Structural Biology 171 2 231 7 doi 10 1016 j jsb 2010 03 020 PMC 2956275 PMID 20371380 Smith FJ Pau VP Cingolani G Rothberg BS December 2012 Crystal structure of a Ba 2 bound gating ring reveals elementary steps in RCK domain activation Structure 20 12 2038 47 doi 10 1016 j str 2012 09 014 PMC 3518701 PMID 23085076 Cao Y Jin X Huang H Derebe MG Levin EJ Kabaleeswaran V Pan Y Punta M Love J Weng J Quick M Ye S Kloss B Bruni R Martinez Hackert E Hendrickson WA Rost B Javitch JA Rajashankar KR Jiang Y Zhou M March 2011 Crystal structure of a potassium ion transporter TrkH Nature 471 7338 336 40 Bibcode 2011Natur 471 336C doi 10 1038 nature09731 PMC 3077569 PMID 21317882 Cao Y Pan Y Huang H Jin X Levin EJ Kloss B Zhou M April 2013 Gating of the TrkH ion channel by its associated RCK protein TrkA Nature 496 7445 317 22 Bibcode 2013Natur 496 317C doi 10 1038 nature12056 PMC 3726529 PMID 23598339 Vieira Pires RS Szollosi A Morais Cabral JH April 2013 The structure of the KtrAB potassium transporter Nature 496 7445 323 8 Bibcode 2013Natur 496 323V doi 10 1038 nature12055 hdl 10216 110345 PMID 23598340 S2CID 205233489 Kong C Zeng W Ye S Chen L Sauer DB Lam Y Derebe MG Jiang Y December 2012 Distinct gating mechanisms revealed by the structures of a multi ligand gated K channel eLife 1 e00184 doi 10 7554 eLife 00184 PMC 3510474 PMID 23240087 Deller MC Johnson HA Miller MD Spraggon G Elsliger MA Wilson IA Lesley SA 2015 Crystal structure of a two subunit TrkA octameric gating ring assembly PLOS ONE 10 3 e0122512 Bibcode 2015PLoSO 1022512D doi 10 1371 journal pone 0122512 PMC 4380455 PMID 25826626 Clayton GM Altieri S Heginbotham L Unger VM Morais Cabral JH February 2008 Structure of the transmembrane regions of a bacterial cyclic nucleotide regulated channel Proceedings of the National Academy of Sciences of the United States of America 105 5 1511 5 Bibcode 2008PNAS 105 1511C doi 10 1073 pnas 0711533105 PMC 2234175 PMID 18216238 Ren D Navarro B Xu H Yue L Shi Q Clapham DE December 2001 A prokaryotic voltage gated sodium channel Science 294 5550 2372 5 Bibcode 2001Sci 294 2372R doi 10 1126 science 1065635 PMID 11743207 S2CID 5721075 Payandeh J Scheuer T Zheng N Catterall WA July 2011 The crystal structure of a voltage gated sodium channel Nature 475 7356 353 8 doi 10 1038 nature10238 PMC 3266868 PMID 21743477 Shaya D Findeisen F Abderemane Ali F Arrigoni C Wong S Nurva SR Loussouarn G Minor DL January 2014 Structure of a prokaryotic sodium channel pore reveals essential gating elements and an outer ion binding site common to eukaryotic channels Journal of Molecular Biology 426 2 467 83 Bibcode 2014BpJ 106 130A doi 10 1016 j jmb 2013 10 010 PMC 3947372 PMID 24120938 Zhang X Ren W DeCaen P Yan C Tao X Tang L Wang J Hasegawa K Kumasaka T He J Wang J Clapham DE Yan N May 2012 Crystal structure of an orthologue of the NaChBac voltage gated sodium channel Nature 486 7401 130 4 Bibcode 2012Natur 486 130Z doi 10 1038 nature11054 PMC 3979295 PMID 22678295 McCusker EC Bagneris C Naylor CE Cole AR D Avanzo N Nichols CG Wallace BA 2012 Structure of a bacterial voltage gated sodium channel pore reveals mechanisms of opening and closing Nature Communications 3 1102 Bibcode 2012NatCo 3 1102M doi 10 1038 ncomms2077 PMC 3493636 PMID 23033078 Shi N Ye S Alam A Chen L Jiang Y March 2006 Atomic structure of a Na and K conducting channel Nature 440 7083 570 4 Bibcode 2006Natur 440 570S doi 10 1038 nature04508 PMID 16467789 S2CID 4355500 Durell SR Guy HR 2001 A family of putative Kir potassium channels in prokaryotes BMC Evolutionary Biology 1 14 doi 10 1186 1471 2148 1 14 PMC 64639 PMID 11806753 Derebe MG Sauer DB Zeng W Alam A Shi N Jiang Y January 2011 Tuning the ion selectivity of tetrameric cation channels by changing the number of ion binding sites Proceedings of the National Academy of Sciences of the United States of America 108 2 598 602 Bibcode 2011PNAS 108 598D doi 10 1073 pnas 1013636108 PMC 3021048 PMID 21187421 Sauer DB Zeng W Raghunathan S Jiang Y October 2011 Protein interactions central to stabilizing the K channel selectivity filter in a four sited configuration for selective K permeation Proceedings of the National Academy of Sciences of the United States of America 108 40 16634 9 Bibcode 2011PNAS 10816634S doi 10 1073 pnas 1111688108 PMC 3189067 PMID 21933962 External links Edit Voltage gated Ion Channels IUPHAR Database of Receptors and Ion Channels International Union of Basic and Clinical Pharmacology This article incorporates text from the public domain Pfam and InterPro IPR005821 Retrieved from https en wikipedia org w index php title Cation channel superfamily amp oldid 1171080289, wikipedia, wiki, book, books, library,

article

, read, download, free, free download, mp3, video, mp4, 3gp, jpg, jpeg, gif, png, picture, music, song, movie, book, game, games.