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Article

Mutation of Walker-A lysine 464 in cystic fibrosis transmembrane conductance regulator reveals functional interaction between its nucleotide-binding domains.

The Journal of physiology - 1 Mar 2002

Powe Allan C, Al-Nakkash Layla, Li Min, Hwang Tzyh-Chang

Abstract excerpt

The cystic fibrosis transmembrane conductance regulator (CFTR) chloride channel bears two nucleotide-binding domains (NBD1 and NBD2) that control its ATP-dependent gating. Exactly how these NBDs control gating is controversial. To address this issue, we examined channels with a Walker-A lysine mutation in NBD1 (K464A) using the patch clamp technique. K464A mutants have an ATP dependence (EC(50) approximate 60...

Topics

3T3 Cells
Adenosine Triphosphate
Adenylyl Imidodiphosphate
Algorithms
Animals
CHO Cells
Cricetinae
Cystic Fibrosis Transmembrane Conductance Regulator
Dose-Response Relationship, Drug
Electrophysiology

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Ion Channel Gating

Ion Channels

Kinetics

Lysine

Mice

Mutation

Nucleotides

Patch-Clamp Techniques

Source

Open in PubMed Open full text

Identifiers

PMID: 11882668
DOI: 10.1113/jphysiol.2001.013162
PMCID: PMC2290141

Genes

PNP
CFTR

Variants

Provenance

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

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Mutation of Walker-A lysine 464 in cystic fibrosis transmembrane conductance regulator reveals functional interaction between its nucleotide-binding domains.PMID 11882668Read ↗

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

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