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Article

Timing of CFTR pore opening and structure of its transition state.

Cell - 22 Oct 2015

Sorum Ben, Czégé Dávid, Csanády László

Abstract excerpt

In CFTR, the chloride ion channel mutated in cystic fibrosis (CF) patients, pore opening is coupled to ATP-binding-induced dimerization of two cytosolic nucleotide binding domains (NBDs) and closure to dimer disruption following ATP hydrolysis. CFTR opening rate, unusually slow because of its high-energy transition state, is further slowed by CF mutation ΔF508. Here, we exploit equilibrium gating of...

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Share to Adenosine Triphosphate
Share to Catalytic Domain
Share to Cystic Fibrosis Transmembrane Conductance Regulator

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to CFTR gene

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Share to Protein Structure, Tertiary

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Source

Identifiers

PMID: 26496611
DOI: 10.1016/j.cell.2015.09.052

Genes

CFTR

Variants

Provenance

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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