2d4z

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2d4z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2d4z OCA], [http://www.ebi.ac.uk/pdbsum/2d4z PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2d4z RCSB]</span>
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[[Category: ion channel regulatory subunit]]
[[Category: ion channel regulatory subunit]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:23:22 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:30:22 2008''

Revision as of 23:30, 30 March 2008


PDB ID 2d4z

Drag the structure with the mouse to rotate
, resolution 3.10Å
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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

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