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Article

Role of Hydrophobic Amino-Acid Side-Chains in the Narrow Selectivity Filter of the CFTR Chloride Channel Pore in Conductance and Selectivity.

The Journal of membrane biology - 1 Dec 2023

Linsdell Paul

Abstract excerpt

Cystic fibrosis is caused by mutations in the cystic fibrosis transmembrane conductance regulator (CFTR) anion channel. Structural analysis of CFTR has identified a narrow, hydrophobic region close to the extracellular end of the open channel pore that may function as a selectivity filter. The present study combines comprehensive mutagenesis of hydrophobic amino-acid side-chains within the selectivity filter with...

Topics

Chloride Channels
Cystic Fibrosis Transmembrane Conductance Regulator
Amino Acids
Mutation
Anions

Source

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Identifiers

PMID: 37823914
DOI: 10.1007/s00232-023-00294-w

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Role of Hydrophobic Amino-Acid Side-Chains in the Narrow Selectivity Filter of the CFTR Chloride Channel Pore in Conductance and Selectivity.PMID 37823914Read ↗

Structural identification of a selectivity filter in CFTRSemantic proximity Read ↗

Two positively charged amino acid side-chains in the inner vestibule of the CFTR channel pore play analogous roles in controlling anion binding and anion conductance.Semantic proximity Read ↗

Direct comparison of the functional roles played by different transmembrane regions in the cystic fibrosis transmembrane conductance regulator chloride channel pore.Semantic proximity Read ↗

Anion conductance selectivity mechanism of the CFTR chloride channel.Semantic proximity Read ↗

Extent of the selectivity filter conferred by the sixth transmembrane region in the CFTR chloride channel pore.Semantic proximity Read ↗

Molecular basis for the chloride channel activity of cystic fibrosis transmembrane conductance regulator and the consequences of disease-causing mutations.Semantic proximity Read ↗

Novel pore-lining residues in CFTR that govern permeation and open-channel block.Semantic proximity Read ↗

Monovalent: Divalent Anion Selectivity in the CFTR Channel Pore.Semantic proximity Read ↗

Structural Changes Fundamental to Gating of the Cystic Fibrosis Transmembrane Conductance Regulator Anion Channel Pore.Semantic proximity Read ↗

Functional differences in pore properties between wild-type and cysteine-less forms of the CFTR chloride channel.Semantic proximity Read ↗

From Selective Permeation to Physiology in Potassium Channels.Semantic proximity Read ↗

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