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TitleCryo-EM Structure of the Open Human Ether-à-go-go-Related K Channel hERG.
Journal, issue, pagesCell, Vol. 169, Issue 3, Page 422-430.e10, Year 2017
Publish dateApr 20, 2017
AuthorsWeiwei Wang / Roderick MacKinnon /
PubMed AbstractThe human ether-à-go-go-related potassium channel (hERG, Kv11.1) is a voltage-dependent channel known for its role in repolarizing the cardiac action potential. hERG alteration by mutation or ...The human ether-à-go-go-related potassium channel (hERG, Kv11.1) is a voltage-dependent channel known for its role in repolarizing the cardiac action potential. hERG alteration by mutation or pharmacological inhibition produces Long QT syndrome and the lethal cardiac arrhythmia torsade de pointes. We have determined the molecular structure of hERG to 3.8 Å using cryo-electron microscopy. In this structure, the voltage sensors adopt a depolarized conformation, and the pore is open. The central cavity has an atypically small central volume surrounded by four deep hydrophobic pockets, which may explain hERG's unusual sensitivity to many drugs. A subtle structural feature of the hERG selectivity filter might correlate with its fast inactivation rate, which is key to hERG's role in cardiac action potential repolarization.
External linksCell / PubMed:28431243 / PubMed Central
MethodsEM (single particle)
Resolution3.7 - 4.0 Å
Structure data

8650

5va1

EMDB-8650, PDB-5va1:
Cryo-EM structure of the human ether-a-go-go related K+ channel
Method: EM (single particle) / Resolution: 3.7 Å

8651

5va2

EMDB-8651, PDB-5va2:
Cryo-EM structure of the human ether-a-go-go related K+ channel
Method: EM (single particle) / Resolution: 3.8 Å

8652

5va3

EMDB-8652, PDB-5va3:
Cryo-EM structure of the human ether-a-go-go related K+ channel
Method: EM (single particle) / Resolution: 4.0 Å

Source
  • homo sapiens (human)
KeywordsTRANSPORT PROTEIN / K+ channel / PAS / CNBHD / voltage sensor / selectivity filter

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