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Article

Mutant cycles at CFTR's non-canonical ATP-binding site support little interface separation during gating.

The Journal of general physiology - 1 Jun 2011

Szollosi Andras, Muallem Daniella R, Csanády László, Vergani Paola

Abstract excerpt

Cystic fibrosis transmembrane conductance regulator (CFTR) is a chloride channel belonging to the adenosine triphosphate (ATP)-binding cassette (ABC) superfamily. ABC proteins share a common molecular mechanism that couples ATP binding and hydrolysis at two nucleotide-binding domains (NBDs) to diverse functions. This involves formation of NBD dimers, with ATP bound at two composite interfacial sites. In CFTR,...

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Source

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Identifiers

PMID: 21576373
DOI: 10.1085/jgp.201110608
PMCID: PMC3105517

Genes

CFTR

Provenance

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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Mutant cycles at CFTR's non-canonical ATP-binding site support little interface separation during gating.PMID 21576373Read ↗

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The two ATP binding sites of cystic fibrosis transmembrane conductance regulator (CFTR) play distinct roles in gating kinetics and energetics.Semantic proximity Read ↗

Strict coupling between CFTR's catalytic cycle and gating of its Cl- ion pore revealed by distributions of open channel burst durations.Semantic proximity Read ↗

Timing of CFTR pore opening and structure of its transition state.Semantic proximity Read ↗

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