Ion channels: Difference between revisions

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</StructureSection>
</StructureSection>
== 3D structures of ion channels ==


Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
{{#tree:id=OrganizedByTopic|openlevels=0|
* Potassium channel See: [[Potassium_Channel#Additional_Structures_of_Potassium_Channels|Potassium Channels]]
* Calcium channel
**[[2d46]] – hVDCC β 4a – human - NMR<br />
**[[6nq0]], [[6nq1]], [[6nq2]] – hTpc2 – Cryo EM  <br />
**[[2f3y]], [[2f3z]], [[2be6]] – hCav1.2 α 1C subunit+calmodulin <br />
**[[3oxq]] - hCav2.1 α 1C subunit IQ domain+hCalmodulin<br />
**[[2vay]], [[3oxq]] - hCav1.1 α 1S subunit IQ domain+hCalmodulin<br />
**[[1hvd]], [[1hve]], [[1hvf]], [[1hvg]] – hAnnexin V (mutant)<br />
**[[6jp5]], [[6jp8]] – rCav1.1 – rabbit – Cryo EM<br />
**[[6jpa]], [[6jpb]] – rCav1.1 + blocker – Cryo EM<br />
**[[3bxx]] – rCav2.1 α 1A subunit+calmodulin - rabbit<br />
**[[3bxl]] - rCav2.3 α 1E subunit+calmodulin<br />
**[[1t0h]] – rVDCC β 2A subunit <br />
**[[1t0j]] – rVDCC β 2A+α 1C <br />
**[[1vyt]] - rVDCC β 3+α 1C <br />
**[[1vyu]] – rVDCC β 3<br />
**[[1vyv]] - rVDCC β 4<br />
**[[1t3l]] - rVDCC β 2+α 1S <br />
**[[1t3s]] - rVDCC β 2<br />
**[[3dve]], [[3dvj]], [[3dvk]], [[3dvm]], [[3g43]] - rCav2.2 α 1B subunit+hCalmodulin<br />
**[[4dex]] - rCav2.2 α 1B + β 2 subunits<br />
**[[4dey]] - rCav2.2 α 1C + β 2 subunits<br />
**[[6byo]] – rCav1.1 α 1S <br />
**[[5gjw]] – rCav1.1 α 2/δ 1 + α 1S +  β 1 – Cryo EM<br />
**[[5gjv]], [[3jbr]] – rCav1.1 α 2/δ 1 + α 1S +  β 1 + γ 1 – Cryo EM<br />
**[[5v2q]], [[5v2p]] - raCav1.2  1C +  2 - rat<br />
**[[5vov]], [[5vou]], [[5vot]], [[5kk2]] - raVDCC g 2 + glutamate receptor – Cryo EM<br />
**[[6c9a]], [[6c96]] – mTpc1 - mouse  <br />
**[[6c96]], [[6c9a]] – mTpc1 – Cryo EM  <br />
**[[4zw2]] – mVDCC α 1S peptide + β 1 <br />
**[[5tua]], [[5e1j]], [[5dqq]] – AtTpc1 – ''Arabidopsis thaliana''  <br />
**[[6cx0]] – AtTpc1 (mutant) <br />
**[[6e1m]], [[6e1n]], [[6e1p]] – AtTpc1 (mutant) – Cryo EM  <br />
**[[6e1k]] – AtTpc1 + antibody – Cryo EM  <br />
**[[6mgv]], [[6mgw]], [[6ijz]] – AtOsca1.2 – Cryo EM  <br />
*See also [[Ryanodine receptor]]
*Sodium channel
**[[2kav]], [[2kbi]] - hNaV 1.2 α C-terminal EF-hand domain - NMR<br />
**[[5fdy]], [[5feb]] - hNaV  2 extracellular domain (mutant)<br />
**[[6agf]] - hNaV  1 + hNav 1.4 – Cryo EM<br />
**[[6j8e]] - hNaV  2 + hNav 1.2 + Mu-conotoxin – Cryo EM<br />
**[[6j8g]], [[6j8h]], [[6j8i]], [[6j8j]] - hNaV  2 + hNaV  1 + hNav 1.7 + toxin – Cryo EM<br />
**[[4l1d]] - hNaV β 3 IG domain <br />
**[[4mz2]] - hNaV β 4 extracellular domain <br />
**[[4mz3]] - hNaV β 4 extracellular domain (mutant)<br />
**[[6mba]], [[6mc9]] – hNaV 1.4  C terminal + calmodulin  <br />
**[[4ovn]], [[5dbr]], [[4djc]], [[6mud]] – hNaV 1.5 α C terminal + calmodulin  <br />
**[[4dck]], [[4jq0]] – hNaV 1.5 α C terminal + calmodulin + fibroblast growth factor <br />
**[[4jpz]] – hNaV 1.2 α C terminal + calmodulin + fibroblast growth factor 13<br />
**[[1byy]] - rNaCh IIA inactivation fragment<br />
**[[5jr0]] – rNaV 1.4    <br />
**[[6mue]] – raNaV 1.4  + calmodulin  <br />
**[[1qg9]] – raNaCh IIA second repeat – NMR<br />
**[[5ayq]], [[5xax]], [[5xaw]] - mNaV  4 residues 30-160 <br />
**[[5xsy]] – eeNaV 1.4 + b 1 – electric eel  - Cryo EM <br />
**[[5x0m]] – coNaCh - cockroach <br />
**[[6a90]], [[6a91]], [[6a95]] – coNaCh + toxin – Cryo EM <br />
**[[4bgn]] – NaCh – ''Caldalkalibacillus thermarum'' – Cryo EM<br />
**[[4lto]], [[4ltp]], [[4ltq]], [[5hk7]] – AeNaCh pore + cytoplasmic domains – ''Alkalilimnicola ehrlichii'' <br />
**[[4ltr]], [[5hkd]], [[5hk6]], [[5kj8]] – AeNaCh pore + cytoplasmic domains (mutant) <br />
**[[5yua]] - AbNaVab – ''Arcobacter butzleri''<br />
**[[5yuc]], [[5yub]] - AbNaVab (mutant) <br />
* NH4+ channel
**[[2nmr]], [[2nop]], [[2now]], [[2npc]], [[2npd]], [[2npe]], [[2npj]], [[2npg]], [[2npk]], [[1u77]], [[1u7c]], [[1u7g]], [[1xqe]], [[1xqf]], [[3c1g]] – EcAmCh – ''Escherichia coli''<br />
**[[3c1h]], [[3c1i]], [[3c1j]] – EcAmCh (mutant)<br />
**[[4nh2]] – EcAmCh + phosphatidylglycerol<br />
**[[2ns1]], [[2nuu]] – EcAmCh + nitrogen regulatory protein<br />
**[[2b2h]], [[2b2i]], [[2b2j]], [[2b2f]] – AmCh – ''Archaeglobus fulgidus''<br />
**[[3b9w]], [[3b9y]], [[3bhs]] – AmCh – ''Nitrosomonas  europaea''
* MscL and MscS
**[[3hzq]] – MscL – ''Staphylococcus aureus''<br />
**[[2oar]] – MscL – ''Mycobacterium tuberculosis''<br />
**[[4lku]] – EcMscL C terminal<br />
**[[4y7k]], [[4y7j]] – MscL – Methanosarcina acetivorans<br />
**[[2oau]], [[2vv5]], [[4hwa]] - EcMscS<br />
**[[4age]], [[4agf]], [[5aji]] – EcMscS (mutant)<br />
**[[3t9n]], [[3udc]] – MscS – ''Thermoanaerobacter tengcongensis''<br />
**[[4hw9]] – MscS – ''Helicobacter pylori''<br />
* Chloride channel
**[[1rk4]], [[3swl]] - hClCh protein 1<br />
**[[6qvu]], [[6qvd]], [[6qvc]], [[6qvb]], [[6qv6]] - hClCh protein 1 – Cryo EM<br />
**[[3o3t]], [[3p8w]], [[3p90]], [[1k0o]], [[3qr6]], [[3tgz]], [[1k0m]], [[3uvh]], [[4iqa]], [[4jzq]], [[4k0g]], [[4k0n]] - hClCh protein 1 (mutant)<br />
**[[6coz]] - hClCh protein 1 C terminal<br />
**[[6coy]] - hClCh protein 1 transmembrane domain<br />
**[[1k0n]] - hClCh protein 1 (mutant) + glutathione<br />
**[[2per]], [[2r4v]], [[2r5g]] - hClCh protein 2<br />
**[[3kjy]], [[3fy7]] - hClCh protein 3 residues 1-230<br />
**[[2ahe]], [[2d2z]] – hClCh protein 4<br />
**[[2pfi]] - hClCh KA<br />
**[[2j9l]], [[2ja3]] - hClCh protein 5 + nucleotide<br />
**[[5tr1]], [[5tqq]] - bCIC (mutant) + antibody – bovine - Cryo EM<br />
**[[6erz]], [[6ery]] - mClCh protein 6<br />
**[[1ots]] - EcERIC + antibody<br />
**[[1ott]], [[1otu]] - EcERIC (mutant) + antibody<br />
**[[2d4z]] - TmClCh - ''Torpedo marmorata''<br />
**[[2yv9]] - CeClCh EXC-4 – ''Caenorhabditis elegans''<br />
**[[3rif]] - CeClCh + antibody + Glu + Ivermectin<br />
**[[5y7i]] - ClCh – ''Oreochromis mossabicus''<br />
*CAMP-dependent chloride channel or cystic fibrosis transmembrane conductance regulator see CFTR in [[ABC transporter 3D structures]]
* Anion Channel (Outer mitochondrial membrane protein porin 1)
**[[2jk4]], [[2k4t]], [[5jdp]], [[5xdo]], [[5xdn]], [[6g73]], [[6g6u]] – hVDAC1<br />
**[[6djb]], [[5zsu]] – hVDAC1 subunit LRRC8A – Cryo EM<br />
**[[3emn]], [[4c69]] – mVDAC1 <br />
**[[6g9o]], [[6g9l]], [[6g8z]], [[6o00]], [[6nzz]], [[6nzw]] – mVDAC1 subunit LRRC8A – Cryo EM<br />
**[[6fnw]] – mVDAC1 subunit LRRC8A C terminal<br />
**[[4bum]] – zeVDAC2 – zebra fish<br />
* Ligand-gated ion channel
**[[2vl0]], [[2yn6]], [[3rqu]] – EchELIC – ''Erwinia chrysanthemi''<br />
**[[2yks]], [[4twh]] - EchELIC (mutant)<br />
**[[3rqw]] - EchELIC + acetylcholine<br />
**[[4twd]], [[4twf]] - EchELIC (mutant) + memantine derivative<br />
**[[3zkr]] - EchELIC + anesthetic<br />
**[[4a97]], [[4a98]] – EchELIC + benzodiazepine<br />
**[[2yoe]] - EchELIC + flurazepam + GABA<br />
**[[5lid]] – EchELIC + bromopromazine <br />
**[[5sxv]] – EchELIC + inhibitor <br />
**[[3eam]], [[3ehz]], [[4hfi]], [[4il4]], [[4ilc]], [[4npp]], [[4npq]], [[4qh1]], [[4qh5]], [[4qh4]], [[6f7a]], [[6f16]], [[4zzc]], [[6hzw]] – GvGLIC – ''Gloeobacter violaceus''br />
**[[3lsv]], [[3tls]], [[3tlt]], [[3tlu]], [[3tlv]], [[3tlw]], [[3uu3]], [[3uu4]], [[3uu5]], [[3uu6]], [[3uu8]], [[3uub]], [[3ei0]], [[4hfb]], [[4il9]], [[4ila]], [[4ilb]], [[4ire]], [[4lmj]], [[4lmk]], [[4lml]], [[5hcj]], [[5hcm]], [[5heg]], [[5heh]], [[5iux]], [[5v6o]], [[5v6n]], [[5nkj]], [[5njy]], [[5mzt]], [[5mzr]], [[5mzq]], [[4zzb]], [[6hy5]], [[6hy9]], [[6hya]], [[6hyr]], [[6hyv]], [[6hyw]], [[6hyx]], [[6hyz]], [[6hz0]], [[6hz1]],  [[6hz3]], [[6emx]], [[6f0i]], [[6f0j]], [[6f0m]], [[6f0n]], [[6f0r]], [[6f0u]], [[6f0v]], [[6f0z]], [[6f10]], [[6f11]], [[6f12]], [[6f13]], [[6f15]], [[6f16]], [[6i08]] – GvGLIC (mutant)<br />
**[[3igq]] – GvGLIC N-terminal<br />
**[[2xq3]], [[2xq4]], [[2xq5]], [[2xq6]], [[2xq7]], [[2xqa]], [[2xq8]] – GvGLIC+inhibitor <br />
**[[2xq9]] – GvGLIC (mutant)+inhibitor<br />
**[[3p4w]], [[3p50]], [[4f8h]], [[4hfh]] – GvGLIC + general anaesthetic<br />
**[[4hfd]], [[5mvn]], [[5mvm]], [[5mur]], [[5muo]] – GvGLIC (mutant) + general anaesthetic<br />
**[[4hfc]], [[4hfe]] - GvGLIC (mutant) + alcohol<br />
**[[5j0z]] - GvGLIC + choline derivative<br />
**[[5l47]], [[5l4e]], [[5l4h]] - GvGLIC + barbiturate<br />
**[[6fl9]], [[6fli]], [[6fvq]], [[6fvr]], [[6fvs]] - STELIC – vent tica<br />
* Cyclic Nucleotide-Gated channel
**[[2zd9]], [[3beh]] - MlCNGC - ''Mesorhizobium loti''<br />
**[[4chv]], [[4chw]] – MlCNGC – Cryo EM<br />
**[[2ptm]] - CNGC C-terminal - ''Strongylocentratus purpuratus''<br />
**[[2kxl]], [[1vp6]] - MlCNGC ligand-binding domain <br />
**[[3co2]], [[4muv]], [[3clp]], [[1u12]] - MlCNGC ligand-binding domain (mutant) <br />
**[[3cl1]], [[2k0g]] - MlCNGC ligand-binding domain + cyclic nucleotide<br />
**[[3swf]] - CNGC CLZ domain - bovine<br />
**[[5h3o]] – CeCNGC – Cryo EM<br />
*Potassium/sodium hyperpolarization-activated cyclic nucleotide-gated channel
**[[3etq]], [[3ffq]],  [[3u0z]], [[3u10]], [[3u11]] - mCNGC C-terminal<br />
**[[1q3e]], [[1q43]], [[1q5o]] - mCNGC 2 fragment + nucleotide<br />
**[[2q0a]] - mCNGC 2 C-terminal (mutant)<br />
**[[3bpz]] - mCNGC 2 ligand-binding domain <br />
**[[5u6o]], [[5u6p]] – hCNGC 1 – Cryo EM<br />
**[[2mpf]] – hCNGC 2 ligand-binding domain - NMR<br />
**[[5khg]], [[5khh]], [[5khi]], [[5khj]], [[5khk]] – mCNGC 2 ligand-binding domain + nucleotide<br />
**[[3swy]] – hCNGC 3 CLZ domain<br />
**[[3otf]] – hCNGC 4 ligand-binding domain<br />
**[[2mng]] – hCNGC 4 ligand-binding domain - NMR<br />
**[[4hbn]] – hCNGC 4 ligand-binding domain (mutant)<br />
**[[4kl1]] – hCNGC 4 C terminal + nucleotide<br />
**[[4nvp]] – hCNGC 4 ligand-binding domain + 7-CH-cAMP<br />
* Acid sensitive ion channel
**[[3ij4]], [[2qts]], [[3s3w]], [[4nyk]], [[3ij4]], [[6ave]], [[5wku]], [[5wkv]], [[5wky]], [[5wkx]], [[6cmc]] – cASC – chicken<br />
**[[3s3x]], [[4fz0]], [[4fz1]] – cASC + psalmotoxin<br />
**[[4ntw]], [[4ntx]], [[4nty]] - cASC + neurotoxin + basic phospholipase A2<br />
* ATP-Gated channel (AGC)
**[[3h9v]], [[3i5d]] – zeAGC <br />
**[[4dw0]] – zeAGC (mutant)<br />
**[[4dw1]] – zeAGC + ATP<br />
* Proton channel or matrix protein 2
**[[2kj1]], [[2l0j]] - IVproton channel – Influenza virus - NMR<br />
**[[2kih]], [[2kwx]] – IVproton channel (mutant)<br />
**[[3bkd]], [[4qkm]], [[4qkl]], [[4qkc]], [[4qk7]], [[3lbw]], [[5ttc]], [[5um1]], [[5joo]] - IVproton channel transmembrane domain<br />
**[[1nyj]], [[1mp6]], [[2kad]] - IVproton channel transmembrane domain - NMR<br />
**[[5c02]], [[4rwc]], [[4rwb]], [[2kih]] - IVproton channel transmembrane domain (mutant)<br />
**[[2n70]] - IVproton channel transmembrane domain (mutant) - NMR<br />
**[[6bkk]], [[6bkl]], [[6bmz]], [[6boc]] - IVproton channel transmembrane domain + drug<br />
**[[2kqt]] - IVproton channel transmembrane domain + drug - NMR<br />
**[[2ly0]] - IVproton channel transmembrane domain (mutant) + drug - NMR<br />
**[[2rtf]] - IVproton channel + inhibitor - NMR<br />
**[[3c9j]] - IVproton channel transmembrane domain + inhibitor<br />
* Voltage-gated hydrogen channel (VGHC)
**[[3a2a]] – hVGHC C-terminal - NMR <br />
**[[5oqk]] – hVGHC residues 82-226 - NMR<br />
**[[3wkv]] – mVGHC <br />
**[[3vmx]], [[3vmy]], [[3vmz]] – mVGHC C-terminal<br />
**[[3vn0]], [[3vyi]] – mVGHC C-terminal (mutant)<br />
*Glycerol facilitator
**[[1lda]], [[1ldi]] - EcGlpF<br />
**[[1fx8]] - EcGlpF + glycerol<br />
**[[1ldf]] - EcGlpF (mutant)
}}
== Weblinks ==
== Weblinks ==
*[http://www.tcdb.org/ The TCDB database]
*[http://www.tcdb.org/ The TCDB database]

Revision as of 11:46, 5 September 2019

Function

Ion channels are membrane proteins that catalyze the passive transport of ions through the cell membrane. Ion channels are the fastest of all membrane transporters, with 106 to 108 transported units per second versus 102 to 104 molecules per second for porters/carriers, or 100 to 103 for ATP-driven pumps.

Ion channel types

Most ion channels are specific to an ion, like the sodium channels, or the Potassium Channel[1].

TRP channels let through various cations[2].
Another property of ion channels is that they can be either driven by voltage or by concentration gradients, or they can be gated (by voltage, ligands, touch and other sensory signal). Potassium channels (KCh) are subdivided to voltage-gated KCh and calcium-dependent KCh. The latter are subdivided into high- (BK, LKCa), intermediate- and small-conductance KCh (human SK1, rat SK2, SKCa). See Potassium channels.
MthK is a calcium-dependent potassium channel from Methanobacterium thermoautrophicum[3].
MscL and MscS are large- and small-conductance mechanosensitive channels which protect bacteria from osmotic shock by allowing ions to flow across the cell membrane[4]. See Mechanosensitive channels: opening and closing.
Voltage-Dependent Calcium Channels (VDCC) allow calcium ions to enter the cell resulting in muscle contraction, neuron excitation or hormone release. VDCC are composed of several subunits and are named as a Cav gene product[5]. See Voltage-gated calcium channels.
There are also Voltage-Dependent Anion Channels (VDAC)[6].
Chloride ion channels (ClCh) are involved in maintaining pH, volume homeostasis and more. The anti-parasitic drug Ivermectin binds to glutamate-gated chloride channels. See Chloride Ion Channel, User:Laura Fountain/Chloride Ion Channel and Chloride Intracellular Channel Protein 2
Ligand-Gated Ion Channels (LGIC) open or close when binding a ligand like a neurotransmitter[7].
Cyclic Nucleotide-Gated channels (CNGC) conduct cations upon binding of cAMP or cGMP[8].
Acid-Sensitive channels (ASC) conduct cations upon binding of acid[9].
Glycerol facilitator (GlpF) is a protein channel which transports glycerol across the cell membrane of E. coli[10].
Other ion channel proteins are the aquaporins, annexin V, gramicidin, antiamoebin, trichotoxin, peptaibol and the glutamate receptor. Specific details in:

Classification

TCDB, the most sophisticated classification of transport proteins to date, classify ion channels as a heterogenous subset of all α-type channels, whose singular property is to consist mainly of α-helices that span the membrane. They are distinct in this from the beta-barrel porins and the pore-forming toxins, as well as from non-ribosomally synthesized channels like gramicidin, polyglutamine or digitoxin. All these proteins are passive transport proteins.

Disease

Mutations in sodium channel are involved in arrhythmia[11], epilepsy[12], Brugada syndrome and cardiac conduction disease[13]. Many diseases are related to voltage-gated sodium, potassium, chloride, acetylcholine and glycine ion channels[14].

Additional Resources

For additional information, see: Membrane Channels & Pumps

For additional information, see: Hypertension & Congestive Heart Failure

3D structures of ion channels

Ion channels 3D structures


Voltage-dependent potassium channel β subunit core complex with NADPH, 1qrq

Drag the structure with the mouse to rotate

WeblinksWeblinks

ReferencesReferences

  1. ↑ Szewczyk A, Jarmuszkiewicz W, Kunz WS. Mitochondrial potassium channels. IUBMB Life. 2009 Feb;61(2):134-43. doi: 10.1002/iub.155. PMID:19165895 doi:http://dx.doi.org/10.1002/iub.155
  2. ↑ Venkatachalam K, Montell C. TRP channels. Annu Rev Biochem. 2007;76:387-417. PMID:17579562 doi:http://dx.doi.org/10.1146/annurev.biochem.75.103004.142819
  3. ↑ Zadek B, Nimigean CM. Calcium-dependent gating of MthK, a prokaryotic potassium channel. J Gen Physiol. 2006 Jun;127(6):673-85. PMID:16735753 doi:http://dx.doi.org/10.1085/jgp.200609534
  4. ↑ Kloda A, Martinac B. Mechanosensitive channels of bacteria and archaea share a common ancestral origin. Eur Biophys J. 2002 Mar;31(1):14-25. PMID:12046893
  5. ↑ Lacinova L. Voltage-dependent calcium channels. Gen Physiol Biophys. 2005 Jun;24 Suppl 1:1-78. PMID:16096350
  6. ↑ Shoshan-Barmatz V, Israelson A, Brdiczka D, Sheu SS. The voltage-dependent anion channel (VDAC): function in intracellular signalling, cell life and cell death. Curr Pharm Des. 2006;12(18):2249-70. PMID:16787253
  7. ↑ Keramidas A, Moorhouse AJ, Schofield PR, Barry PH. Ligand-gated ion channels: mechanisms underlying ion selectivity. Prog Biophys Mol Biol. 2004 Oct;86(2):161-204. PMID:15288758 doi:http://dx.doi.org/10.1016/j.pbiomolbio.2003.09.002
  8. ↑ Kaupp UB, Seifert R. Cyclic nucleotide-gated ion channels. Physiol Rev. 2002 Jul;82(3):769-824. PMID:12087135 doi:http://dx.doi.org/10.1152/physrev.00008.2002
  9. ↑ Holzer P. Acid-sensitive ion channels and receptors. Handb Exp Pharmacol. 2009;(194):283-332. doi: 10.1007/978-3-540-79090-7_9. PMID:19655111 doi:http://dx.doi.org/10.1007/978-3-540-79090-7_9
  10. ↑ Stroud RM, Miercke LJ, O'Connell J, Khademi S, Lee JK, Remis J, Harries W, Robles Y, Akhavan D. Glycerol facilitator GlpF and the associated aquaporin family of channels. Curr Opin Struct Biol. 2003 Aug;13(4):424-31. PMID:12948772
  11. ↑ Ruan Y, Liu N, Priori SG. Sodium channel mutations and arrhythmias. Nat Rev Cardiol. 2009 May;6(5):337-48. doi: 10.1038/nrcardio.2009.44. PMID:19377496 doi:http://dx.doi.org/10.1038/nrcardio.2009.44
  12. ↑ Meisler MH, Kearney JA. Sodium channel mutations in epilepsy and other neurological disorders. J Clin Invest. 2005 Aug;115(8):2010-7. PMID:16075041 doi:http://dx.doi.org/10.1172/JCI25466
  13. ↑ Watanabe H, Koopmann TT, Le Scouarnec S, Yang T, Ingram CR, Schott JJ, Demolombe S, Probst V, Anselme F, Escande D, Wiesfeld AC, Pfeufer A, Kaab S, Wichmann HE, Hasdemir C, Aizawa Y, Wilde AA, Roden DM, Bezzina CR. Sodium channel beta1 subunit mutations associated with Brugada syndrome and cardiac conduction disease in humans. J Clin Invest. 2008 Jun;118(6):2260-8. doi: 10.1172/JCI33891. PMID:18464934 doi:http://dx.doi.org/10.1172/JCI33891
  14. ↑ Dworakowska B, Dolowy K. Ion channels-related diseases. Acta Biochim Pol. 2000;47(3):685-703. PMID:11310970

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