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Article

Folding studies of Cox17 reveal an important interplay of cysteine oxidation and copper binding.

Structure (London, England : 1993) - 1 May 2005

Arnesano Fabio, Balatri Erica, Banci Lucia, Bertini Ivano, Winge Dennis R

Abstract excerpt

Cox17 is a key mitochondrial copper chaperone involved in the assembly of cytochrome c oxidase (COX). The NMR solution structure of the oxidized apoCox17 isoform consists of a coiled-coil conformation stabilized by two disulfide bonds involving Cys(26)/Cys(57) and Cys(36)/Cys(47). This appears to be a conserved tertiary fold of a class of proteins, localized within the mitochondrial intermembrane space, that...

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Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

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Identifiers

PMID: 15893662
DOI: 10.1016/j.str.2005.02.015

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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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