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Article

Removal of gating in voltage-dependent ClC-2 chloride channel by point mutations affecting the pore and C-terminus CBS-2 domain.

The Journal of physiology - 1 Apr 2006

Yusef Yamil R, Zúñiga Leandro, Catalán Marcelo, Niemeyer María Isabel, Cid L Pablo, Sepúlveda Francisco V

Abstract excerpt

Functional and structural studies demonstrate that Cl(-) channels of the ClC family have a dimeric double-barrelled structure, with each monomer contributing an identical pore. Studies with ClC-0, the prototype ClC channel, show the presence of independent mechanisms gating the individual pores or both pores simultaneously. A single-point mutation in the CBS-2 domain of ClC-0 has been shown to abolish slow...

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Identifiers

PMID: 16469788
DOI: 10.1113/jphysiol.2005.102392
PMCID: PMC1779660

Genes

CBS

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.

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