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Article

Two critical cysteine residues implicated in disulfide bond formation and proper folding of Kir2.1.

Biochemistry - 25 Apr 2000

Cho H C, Tsushima R G, Nguyen T T, Guy H R, Backx P H

Abstract excerpt

Inwardly rectifying potassium channels are important in cellular repolarization of many excitable tissues. Amino acid sequence alignment of different mammalian inward rectifier K(+) channels revealed two absolutely conserved cysteine residues in the putative extracellular face, suggesting a possible disulfide bond. Replacement of these cysteine residues in the Kir2.1 channel (i.e., C122 and C154) with either...

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Identifiers

PMID: 10769120
DOI: 10.1021/bi992469g

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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