9CHR
Cryo-EM structure of the human ether-a-go-go related K+ channel (hERG) in 300 mM K+ without symmetry
Summary for 9CHR
| Entry DOI | 10.2210/pdb9chr/pdb |
| Related | 9CHP 9CHQ |
| EMDB information | 45599 |
| Descriptor | Potassium voltage-gated channel subfamily H member 2 (1 entity in total) |
| Functional Keywords | ion channel, membrane protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 4 |
| Total formula weight | 350733.41 |
| Authors | Lau, C.H.Y.,Hunter, M.J.,Vandenberg, J.I. (deposition date: 2024-07-01, release date: 2024-08-21, Last modification date: 2024-09-11) |
| Primary citation | Lau, C.H.Y.,Flood, E.,Hunter, M.J.,Williams-Noonan, B.J.,Corbett, K.M.,Ng, C.A.,Bouwer, J.C.,Stewart, A.G.,Perozo, E.,Allen, T.W.,Vandenberg, J.I. Potassium dependent structural changes in the selectivity filter of HERG potassium channels. Nat Commun, 15:7470-7470, 2024 Cited by PubMed Abstract: The fine tuning of biological electrical signaling is mediated by variations in the rates of opening and closing of gates that control ion flux through different ion channels. Human ether-a-go-go related gene (HERG) potassium channels have uniquely rapid inactivation kinetics which are critical to the role they play in regulating cardiac electrical activity. Here, we exploit the K sensitivity of HERG inactivation to determine structures of both a conductive and non-conductive selectivity filter structure of HERG. The conductive state has a canonical cylindrical shaped selectivity filter. The non-conductive state is characterized by flipping of the selectivity filter valine backbone carbonyls to point away from the central axis. The side chain of S620 on the pore helix plays a central role in this process, by coordinating distinct sets of interactions in the conductive, non-conductive, and transition states. Our model represents a distinct mechanism by which ion channels fine tune their activity and could explain the uniquely rapid inactivation kinetics of HERG. PubMed: 39209832DOI: 10.1038/s41467-024-51208-w PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.5 Å) |
Structure validation
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