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'''Crystal structure of the cytoplasmic domain of the chloride channel ClC-0''' | '''Crystal structure of the cytoplasmic domain of the chloride channel ClC-0''' | ||
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[[Category: Dutzler, R.]] | [[Category: Dutzler, R.]] | ||
[[Category: Meyer, S.]] | [[Category: Meyer, S.]] | ||
[[Category: | [[Category: Cbs domain]] | ||
[[Category: | [[Category: Clc chloride channel cytoplasmic domain]] | ||
[[Category: | [[Category: Ion channel regulatory subunit]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 23:42:57 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 20:42, 3 May 2008
Crystal structure of the cytoplasmic domain of the chloride channel ClC-0
Overview
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.
About this Structure
2D4Z is a Single protein structure of sequence from Torpedo marmorata. Full crystallographic information is available from OCA.
Reference
Crystal structure of the cytoplasmic domain of the chloride channel ClC-0., Meyer S, Dutzler R, Structure. 2006 Feb;14(2):299-307. PMID:16472749 Page seeded by OCA on Sat May 3 23:42:57 2008
