CFTR channel opening by ATP-driven tight dimerization of its nucleotide-binding domains.

doi:10.1038/nature03313

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Article

CFTR channel opening by ATP-driven tight dimerization of its nucleotide-binding domains.

Nature - 24 Feb 2005

Vergani Paola, Lockless Steve W, Nairn Angus C, Gadsby David C

Abstract excerpt

ABC (ATP-binding cassette) proteins constitute a large family of membrane proteins that actively transport a broad range of substrates. Cystic fibrosis transmembrane conductance regulator (CFTR), the protein dysfunctional in cystic fibrosis, is unique among ABC proteins in that its transmembrane domains comprise an ion channel. Opening and closing of the pore have been linked to ATP binding and hydrolysis at...

Topics

Adenosine Triphosphate
Catalytic Domain
Cystic Fibrosis Transmembrane Conductance Regulator
Dimerization
Electrophysiology
Humans
Hydrolysis
Ion Channel Gating
Mutation
Protein Binding
Protein Structure, Quaternary
Protein Structure, Tertiary
Thermodynamics

Source

Open in PubMed Open full text

Identifiers

PMID: 15729345
DOI: 10.1038/nature03313
PMCID: PMC2756053

Genes

CFTR

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 31 Aug 2026.

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