1pzd is a 1 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Hoffman GR, Rahl PB, Collins RN, Cerione RA. Conserved structural motifs in intracellular trafficking pathways: structure of the gammaCOP appendage domain. Mol Cell. 2003 Sep;12(3):615-25. PMID:14527408
