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Article

Probing the molecular basis of hERG drug block with unnatural amino acids.

Scientific reports - 10 Jan 2018

Macdonald Logan C, Kim Robin Y, Kurata Harley T, Fedida David

Abstract excerpt

Repolarization of the cardiac action potential is primarily mediated by two voltage-dependent potassium currents: I Kr and I Ks . The voltage-gated potassium channel that gives rise to I Kr, Kv11.1 (hERG), is uniquely susceptible to high-affinity block by a wide range of drug classes. Pore residues Tyr652 and Phe656 are critical to potent drug interaction with hERG. It is considered that the molecular basis of...

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Identifiers

PMID: 29321549
DOI: 10.1038/s41598-017-18448-x
PMCID: PMC5762913

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Probing the molecular basis of hERG drug block with unnatural amino acids.PMID 29321549Read ↗

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