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Article

Walker mutations reveal loose relationship between catalytic and channel-gating activities of purified CFTR (cystic fibrosis transmembrane conductance regulator).

Biochemistry - 2 Feb 1999

Ramjeesingh M, Li C, Garami E, Huan L J, Galley K, Wang Y, Bear C E

Abstract excerpt

The cystic fibrosis transmembrane conductance regulator (CFTR) functions as an ATPase and as a chloride channel. It has been hypothesized, on the basis of electrophysiological findings, that the catalytic activity of CFTR is tightly coupled to the opening and closing of the channel gate. In the present study, to determine the structural basis for the ATPase activity of CFTR, we assessed the effect of mutations...

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Source

Identifiers

PMID: 9931011
DOI: 10.1021/bi982243y

Genes

CFTR

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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.

Related research

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Walker mutations reveal loose relationship between catalytic and channel-gating activities of purified CFTR (cystic fibrosis transmembrane conductance regulator).PMID 9931011Read ↗

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Electrophysiological, biochemical, and bioinformatic methods for studying CFTR channel gating and its regulation.Semantic proximity Read ↗

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G551D and G1349D, Two CF-associated Mutations in the Signature Sequences of CFTR, Exhibit Distinct Gating DefectsSemantic proximity Read ↗

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

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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 ↗

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