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TitleCryo-EM Structure of K-Bound hERG Channel Complexed with the Blocker Astemizole.
Journal, issue, pagesStructure, Vol. 29, Issue 3, Page 203-212.e4, Year 2021
Publish dateMar 4, 2021
AuthorsTatsuki Asai / Naruhiko Adachi / Toshio Moriya / Hideyuki Oki / Takamitsu Maru / Masato Kawasaki / Kano Suzuki / Sisi Chen / Ryohei Ishii / Kazuko Yonemori / Shigeru Igaki / Satoshi Yasuda / Satoshi Ogasawara / Toshiya Senda / Takeshi Murata /
PubMed AbstractThe hERG channel is a voltage-gated potassium channel involved in cardiac repolarization. Off-target hERG inhibition by drugs has become a critical issue in the pharmaceutical industry. The three- ...The hERG channel is a voltage-gated potassium channel involved in cardiac repolarization. Off-target hERG inhibition by drugs has become a critical issue in the pharmaceutical industry. The three-dimensional structure of the hERG channel was recently reported at 3.8-Å resolution using cryogenic electron microscopy (cryo-EM). However, the drug inhibition mechanism remains unclear because of the scarce structural information regarding the drug- and potassium-bound hERG channels. In this study, we obtained the cryo-EM density map of potassium-bound hERG channel complexed with astemizole, a well-known hERG inhibitor that increases risk of potentially fatal arrhythmia, at 3.5-Å resolution. The structure suggested that astemizole inhibits potassium conduction by binding directly below the selectivity filter. Furthermore, we propose a possible binding model of astemizole to the hERG channel and provide insights into the unusual sensitivity of hERG to several drugs.
External linksStructure / PubMed:33450182
MethodsEM (single particle)
Resolution3.7 - 3.9 Å
Structure data

30412

7cn0

EMDB-30412, PDB-7cn0:
Cryo-EM structure of K+-bound hERG channel
Method: EM (single particle) / Resolution: 3.9 Å

30413

7cn1

EMDB-30413, PDB-7cn1:
Cryo-EM structure of K+-bound hERG channel in the presence of astemizole
Method: EM (single particle) / Resolution: 3.7 Å

Chemicals

ChemComp-K:
Unknown entry

Source
  • homo sapiens (human)
KeywordsTRANSPORT PROTEIN / potassium channel

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