2yv7: Difference between revisions

Revision as of 19:38, 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:2yv7.png

Template:STRUCTURE 2yv7

Crystal structure of the CLIC homolog from drosophila melanogasterCrystal structure of the CLIC homolog from drosophila melanogaster

Template:ABSTRACT PUBMED 17985355

About this StructureAbout this Structure

2YV7 is a Single protein structure of sequence from Drosophila melanogaster. Full crystallographic information is available from OCA.

ReferenceReference

Comparison of vertebrate and invertebrate CLIC proteins: The crystal structures of Caenorhabditis elegans EXC-4 and Drosophila melanogaster DmCLIC., Littler DR, Harrop SJ, Brown LJ, Pankhurst GJ, Mynott AV, Luciani P, Mandyam RA, Mazzanti M, Tanda S, Berryman MA, Breit SN, Curmi PM, Proteins. 2007 Oct 23;71(1):364-378. PMID:17985355

Page seeded by OCA on Mon Jul 28 19:37:53 2008

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

OCA

@@ Line 1: / Line 1: @@
-[[Image:2yv7.jpg|left|200px]]
+{{Seed}}
+[[Image:2yv7.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_2yv7|  PDB=2yv7  |  SCENE=  }}
-'''Crystal structure of the CLIC homolog from drosophila melanogaster'''
+===Crystal structure of the CLIC homolog from drosophila melanogaster===
-==Overview==
+<!--
-The crystal structures of two CLIC family members DmCLIC and EXC-4 from the invertebrates Drosophila melanogaster and Caenorhabditis elegans, respectively, have been determined. The proteins adopt a glutathione S-transferase (GST) fold. The structures are highly homologous to each other and more closely related to the known structures of the human CLIC1 and CLIC4 than to GSTs. The invertebrate CLICs show several unique features including an elongated C-terminal extension and a divalent metal binding site. The latter appears to alter the ancestral glutathione binding site, and thus, the invertebrate CLICs are unlikely to bind glutathione in the same manner as the GST proteins. Purified recombinant DmCLIC and EXC-4 both bind to lipid bilayers and can form ion channels in artificial lipid bilayers, albeit at low pH. EXC-4 differs from other CLIC proteins in that the conserved redox-active cysteine at the N-terminus of helix 1 is replaced by an aspartic acid residue. Other key distinguishing features of EXC-4 include the fact that it binds to artificial bilayers at neutral pH and this binding is not sensitive to oxidation. These differences with other CLIC family members are likely to be due to the substitution of the conserved cysteine by aspartic acid. Proteins 2008. (c) 2007 Wiley-Liss, Inc.
+The line below this paragraph, {{ABSTRACT_PUBMED_17985355}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 17985355 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_17985355}}
 ==About this Structure==
@@ Line 30: / Line 34: @@
 [[Category: Gst fold]]
 [[Category: Metal transport]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 19:31:02 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 19:37:53 2008''