Referenced in: none

Automatically associated channels: ClC4

Title: Crystal structure of the cytoplasmic domain of the chloride channel ClC-0.

Authors: Sebastian Meyer, Raimund Dutzler

Journal, date & volume: Structure, 2006 Feb , 14, 299-307

PubMed link: http://www.ncbi.nlm.nih.gov/pubmed/16472749

Abstract
Ion channels are frequently organized in a modular fashion and consist of a membrane-embedded pore domain and a soluble regulatory domain. A similar organization is found for the ClC family of Cl- channels and transporters. Here, we describe the crystal structure of the cytoplasmic domain of ClC-0, the voltage-dependent Cl- channel from T. marmorata. The structure contains a folded core of two tightly interacting cystathionine beta-synthetase (CBS) subdomains. The two subdomains are connected by a 96 residue mobile linker that is disordered in the crystals. As revealed by analytical ultracentrifugation, the domains form dimers, thereby most likely extending the 2-fold symmetry of the transmembrane pore. The structure provides insight into the organization of the cytoplasmic domains within the ClC family and establishes a framework for guiding future investigations on regulatory mechanisms.