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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 3.10&Aring;" /> '''Crystal structure of...)
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[[Image:2d4z.gif|left|200px]]<br /><applet load="2d4z" size="350" color="white" frame="true" align="right" spinBox="true"
caption="2d4z, resolution 3.10&Aring;" />
caption="2d4z, resolution 3.10&Aring;" />
'''Crystal structure of the cytoplasmic domain of the chloride channel ClC-0'''<br />
'''Crystal structure of the cytoplasmic domain of the chloride channel ClC-0'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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2D4Z is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Torpedo_marmorata Torpedo marmorata]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2D4Z OCA].
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2D4Z is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Torpedo_marmorata Torpedo marmorata]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D4Z OCA].
==Reference==
==Reference==
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[[Category: ion channel regulatory subunit]]
[[Category: ion channel regulatory subunit]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 09:26:49 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:55:28 2008''

Revision as of 14:55, 21 February 2008


2d4z, resolution 3.10Å

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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 Thu Feb 21 16:55:28 2008

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