2ahe: Difference between revisions

Revision as of 07:41, 28 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2ahe.png

Template:STRUCTURE 2ahe

Crystal structure of a soluble form of CLIC4. intercellular chloride ion channelCrystal structure of a soluble form of CLIC4. intercellular chloride ion channel

Template:ABSTRACT PUBMED 16176272

About this StructureAbout this Structure

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

ReferenceReference

Crystal structure of the soluble form of the redox-regulated chloride ion channel protein CLIC4., Littler DR, Assaad NN, Harrop SJ, Brown LJ, Pankhurst GJ, Luciani P, Aguilar MI, Mazzanti M, Berryman MA, Breit SN, Curmi PM, FEBS J. 2005 Oct;272(19):4996-5007. PMID:16176272

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-'''Crystal structure of a soluble form of CLIC4. intercellular chloride ion channel'''
+===Crystal structure of a soluble form of CLIC4. intercellular chloride ion channel===
-==Overview==
+<!--
-The structure of CLIC4, a member of the CLIC family of putative intracellular chloride ion channel proteins, has been determined at 1.8 Angstroms resolution by X-ray crystallography. The protein is monomeric and it is structurally similar to CLIC1, belonging to the GST fold class. Differences between the structures of CLIC1 and CLIC4 are localized to helix 2 in the glutaredoxin-like N-terminal domain, which has previously been shown to undergo a dramatic structural change in CLIC1 upon oxidation. The structural differences in this region correlate with the sequence differences, where the CLIC1 sequence appears to be atypical of the family. Purified, recombinant, wild-type CLIC4 is shown to bind to artificial lipid bilayers, induce a chloride efflux current when associated with artificial liposomes and produce an ion channel in artificial bilayers with a conductance of 30 pS. Membrane binding is enhanced by oxidation of CLIC4 while no channels were observed via tip-dip electrophysiology in the presence of a reducing agent. Thus, recombinant CLIC4 appears to be able to form a redox-regulated ion channel in the absence of any partner proteins.
+The line below this paragraph, {{ABSTRACT_PUBMED_16176272}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16176272 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_16176272}}
 ==About this Structure==
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 [[Category: Glutathione-s-transferase superfamily]]
 [[Category: Ncc27]]
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