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TitleStructural Basis for Pore Blockade of the Human Cardiac Sodium Channel Na 1.5 by the Antiarrhythmic Drug Quinidine*.
Journal, issue, pagesAngew Chem Int Ed Engl, Vol. 60, Issue 20, Page 11474-11480, Year 2021
Publish dateMay 10, 2021
AuthorsZhangqiang Li / Xueqin Jin / Tong Wu / Gaoxingyu Huang / Kun Wu / Jianlin Lei / Xiaojing Pan / Nieng Yan /
PubMed AbstractNa 1.5, the primary voltage-gated Na (Na ) channel in heart, is a major target for class I antiarrhythmic agents. Here we present the cryo-EM structure of full-length human Na 1.5 bound to quinidine, ...Na 1.5, the primary voltage-gated Na (Na ) channel in heart, is a major target for class I antiarrhythmic agents. Here we present the cryo-EM structure of full-length human Na 1.5 bound to quinidine, a class Ia antiarrhythmic drug, at 3.3 Å resolution. Quinidine is positioned right beneath the selectivity filter in the pore domain and coordinated by residues from repeats I, III, and IV. Pore blockade by quinidine is achieved through both direct obstruction of the ion permeation path and induced rotation of an invariant Tyr residue that tightens the intracellular gate. Structural comparison with a truncated rat Na 1.5 in the presence of flecainide, a class Ic agent, reveals distinct binding poses for the two antiarrhythmics within the pore domain. Our work reported here, along with previous studies, reveals the molecular basis for the mechanism of action of class I antiarrhythmic drugs.
External linksAngew Chem Int Ed Engl / PubMed:33684260
MethodsEM (single particle)
Resolution3.3 Å
Structure data

0942

6lqa

EMDB-0942, PDB-6lqa:
voltage-gated sodium channel Nav1.5 with quinidine
Method: EM (single particle) / Resolution: 3.3 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-QDN:
Quinidine / antiarrhythmic*YM

Source
  • homo sapiens (human)
KeywordsTRANSPORT PROTEIN / membrane protein / Voltage-gated sodium channel

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