2d4z: Difference between revisions
New page: left|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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[[Image:2d4z.gif|left|200px]]<br /><applet load="2d4z" size=" | [[Image:2d4z.gif|left|200px]]<br /><applet load="2d4z" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2d4z, resolution 3.10Å" /> | caption="2d4z, resolution 3.10Å" /> | ||
'''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== | ||
Ion channels are frequently organized in a modular fashion and consist of | 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== | ||
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:// | 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]] | ||
''Page seeded by [http:// | ''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
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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
