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Article

Four basic residues critical for the ion selectivity and pore blocker sensitivity of TMEM16A calcium-activated chloride channels.

Proceedings of the National Academy of Sciences of the United States of America - 17 Mar 2015

Peters Christian J, Yu Haibo, Tien Jason, Jan Yuh Nung, Li Min, Jan Lily Yeh

Abstract excerpt

TMEM16A (transmembrane protein 16) (Anoctamin-1) forms a calcium-activated chloride channel (CaCC) that regulates a broad array of physiological properties in response to changes in intracellular calcium concentration. Although known to conduct anions according to the Eisenman type I selectivity sequence, the structural determinants of TMEM16A anion selectivity are not well-understood. Reasoning that the positive...

Topics

Alanine
Amino Acids, Basic
Animals
Anions
Anoctamin-1
Calcium
Cell Membrane Permeability
Chloride Channels
HEK293 Cells
High-Throughput Screening Assays

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Humans

Ion Channel Gating

Mice

Models, Molecular

Mutation

Patch-Clamp Techniques

Small Molecule Libraries

Structure-Activity Relationship

Source

Open in PubMed Open full text

Identifiers

PMID: 25733897
DOI: 10.1073/pnas.1502291112
PMCID: PMC4371966

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 30 Aug 2026.

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Four basic residues critical for the ion selectivity and pore blocker sensitivity of TMEM16A calcium-activated chloride channels.PMID 25733897Read ↗

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