5VA3
Cryo-EM structure of the human ether-a-go-go related K+ channel
Summary for 5VA3
| Entry DOI | 10.2210/pdb5va3/pdb |
| Related | 5VA1 5VA2 |
| EMDB information | 8650 8651 8652 |
| Descriptor | Potassium voltage-gated channel subfamily H member 2 (1 entity in total) |
| Functional Keywords | k+ channel, pas, cnbhd, voltage sensor, selectivity filter, transport protein |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 1 |
| Total formula weight | 88885.66 |
| Authors | Wang, W.W.,MacKinnon, R. (deposition date: 2017-03-24, release date: 2017-05-03, Last modification date: 2024-03-13) |
| Primary citation | Wang, W.,MacKinnon, R. Cryo-EM Structure of the Open Human Ether-a-go-go-Related K(+) Channel hERG. Cell, 169:422-430.e10, 2017 Cited by PubMed Abstract: 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. PubMed: 28431243DOI: 10.1016/j.cell.2017.03.048 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4 Å) |
Structure validation
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