Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

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.

Cellular and molecular life sciences : CMLS - 1 Jun 2021

Linsdell Paul, Irving Christina L, Cowley Elizabeth A, El Hiani Yassine

Abstract excerpt

Positively charged amino acid side-chains play important roles in anion binding and permeation through the CFTR chloride channel. One pore-lining lysine residue in particular (K95) has been shown to be indispensable for anion binding, conductance, and selectivity. Here, we use functional investigation of CFTR to show that a nearby arginine (R134) plays a functionally analogous role. Removal of this positive...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Anions
Share to Arginine

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Cells, Cultured

Share to Cricetinae

Share to Cystic Fibrosis Transmembrane Conductance Regulator

Share to Lysine

Share to Patch-Clamp Techniques

Share to Protein Conformation

Source

Open in PubMed Open full text

Identifiers

PMID: 34023918
DOI: 10.1007/s00018-021-03859-x
PMCID: PMC11073087

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.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

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.PMID 34023918Read ↗

Identification of positive charges situated at the outer mouth of the CFTR chloride channel pore.Semantic proximity Read ↗

Cystic fibrosis-associated mutations at arginine 347 alter the pore architecture of CFTR. Evidence for disruption of a salt bridge.Semantic proximity Read ↗

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

Positive charges at the intracellular mouth of the pore regulate anion conduction in the CFTR chloride channel.Semantic proximity Read ↗

Structural identification of a selectivity filter in CFTRSemantic proximity Read ↗

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

Interactions between permeant and blocking anions inside the CFTR chloride channel pore.Semantic proximity Read ↗

Molecular determinants and role of an anion binding site in the external mouth of the CFTR chloride 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 ↗

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

Cystic fibrosis transmembrane conductance regulator. Physical basis for lyotropic anion selectivity patterns.Semantic proximity Read ↗

Cystic Fibrosis Transmembrane Conductance Regulator (CFTR)Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.