1pzd
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(New page: 200px<br /><applet load="1pzd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pzd, resolution 2.31Å" /> '''Structural Identific...)
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Revision as of 22:08, 20 November 2007
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Structural Identification of a conserved appendage domain in the carboxyl-terminus of the COPI gamma-subunit.
Overview
The formation of coated vesicles is a fundamental step in many, intracellular trafficking pathways. COPI and clathrin represent two, important and distinct sets of vesicle coating machinery, involved, primarily in mediating intra-Golgi and endocytic transport, respectively., Here we identify an important functional region at the carboxyl terminus, of the gamma subunit of the COPI complex (gammaCOP) and describe the X-ray, crystal structure of this domain at 2.3 A resolution. This domain of, gammaCOP exhibits unexpected structural similarity to the, carboxyl-terminal appendage domains of the alpha and beta subunits of the, AP2 adaptor proteins, integral components of clathrin-coated vesicles. The, remarkable structural conservation exhibited by the gammaCOP appendage, domain, coupled with functional data and primary sequence analysis, supports a model of COPI function with significant structural and, mechanistic parallels to vesicular transport by the clathrin/AP2 system.
About this Structure
1PZD is a Single protein structure of sequence from Bos taurus with SO4 as ligand. Full crystallographic information is available from OCA.
Reference
Conserved structural motifs in intracellular trafficking pathways: structure of the gammaCOP appendage domain., Hoffman GR, Rahl PB, Collins RN, Cerione RA, Mol Cell. 2003 Sep;12(3):615-25. PMID:14527408
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