2d2z

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(New page: 200px<br /> <applet load="2d2z" size="450" color="white" frame="true" align="right" spinBox="true" caption="2d2z, resolution 2.2&Aring;" /> '''Crystal structure of...)
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caption="2d2z, resolution 2.2&Aring;" />
caption="2d2z, resolution 2.2&Aring;" />
'''Crystal structure of Soluble Form Of CLIC4'''<br />
'''Crystal structure of Soluble Form Of CLIC4'''<br />
==Overview==
==Overview==
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The crystal structure of a wild type of the human soluble chloride, intracellular ion channel CLIC4 (wCLIC4) has been determined at a, resolution of 2.2A. The structure shows a homotrimer in an asymmetric, unit, which is first observed in CLICs. The assembly of the trimer takes a, unique triple interaction mode between three monomers with a hydrogen-bond, network and hydrophobic contacts. Through such complicated interactions, the homotrimer of wCLIC4 is firmly stabilized. The structure shows an, oligomeric mode with a unique assembly mechanism by which the, oligomerization of CLIC4 can be performed without any intramolecular, disulfide bond formation. It indicated a possibility that CLIC4 may take a, unique structural organization distinct from CLIC1 for docking with lipid, bilayers. In addition, the structure shows distinct conformational states, of the h2 region for respective monomers of the trimer, which reveal an, intrinsic conformational susceptibility for this significant region in the, structural transition.
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The crystal structure of a wild type of the human soluble chloride intracellular ion channel CLIC4 (wCLIC4) has been determined at a resolution of 2.2A. The structure shows a homotrimer in an asymmetric unit, which is first observed in CLICs. The assembly of the trimer takes a unique triple interaction mode between three monomers with a hydrogen-bond network and hydrophobic contacts. Through such complicated interactions, the homotrimer of wCLIC4 is firmly stabilized. The structure shows an oligomeric mode with a unique assembly mechanism by which the oligomerization of CLIC4 can be performed without any intramolecular disulfide bond formation. It indicated a possibility that CLIC4 may take a unique structural organization distinct from CLIC1 for docking with lipid bilayers. In addition, the structure shows distinct conformational states of the h2 region for respective monomers of the trimer, which reveal an intrinsic conformational susceptibility for this significant region in the structural transition.
==About this Structure==
==About this Structure==
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2D2Z is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2D2Z OCA].
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2D2Z is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2D2Z OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Li, D.F.]]
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[[Category: Li, D F.]]
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[[Category: Li, Y.F.]]
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[[Category: Li, Y F.]]
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[[Category: Wang, D.C.]]
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[[Category: Wang, D C.]]
[[Category: clic4]]
[[Category: clic4]]
[[Category: crystal structure]]
[[Category: crystal structure]]
[[Category: soluble form]]
[[Category: soluble form]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 21:25:42 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:54:51 2008''

Revision as of 14:54, 21 February 2008


2d2z, resolution 2.2Å

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Crystal structure of Soluble Form Of CLIC4

Overview

The crystal structure of a wild type of the human soluble chloride intracellular ion channel CLIC4 (wCLIC4) has been determined at a resolution of 2.2A. The structure shows a homotrimer in an asymmetric unit, which is first observed in CLICs. The assembly of the trimer takes a unique triple interaction mode between three monomers with a hydrogen-bond network and hydrophobic contacts. Through such complicated interactions, the homotrimer of wCLIC4 is firmly stabilized. The structure shows an oligomeric mode with a unique assembly mechanism by which the oligomerization of CLIC4 can be performed without any intramolecular disulfide bond formation. It indicated a possibility that CLIC4 may take a unique structural organization distinct from CLIC1 for docking with lipid bilayers. In addition, the structure shows distinct conformational states of the h2 region for respective monomers of the trimer, which reveal an intrinsic conformational susceptibility for this significant region in the structural transition.

About this Structure

2D2Z is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Trimeric structure of the wild soluble chloride intracellular ion channel CLIC4 observed in crystals., Li Y, Li D, Zeng Z, Wang D, Biochem Biophys Res Commun. 2006 May 19;343(4):1272-8. Epub 2006 Mar 27. PMID:16581025

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