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2d4z
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(New page: 200px<br /><applet load="2d4z" size="450" color="white" frame="true" align="right" spinBox="true" caption="2d4z, resolution 3.10Å" /> '''Crystal structure of...)
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Revision as of 07:19, 21 November 2007
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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 Wed Nov 21 09:26:49 2007
