1r4x
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Crystal Structure Analys of the Gamma-COPI Appendage domain
OverviewOverview
COPI-coated vesicles mediate retrograde transport from the Golgi back to, the ER and intra-Golgi transport. The cytosolic precursor of the COPI, coat, the heptameric coatomer complex, can be thought of as composed of, two subcomplexes. The first consists of the beta-, gamma-, delta- and, zeta-COP subunits which are distantly homologous to AP clathrin adaptor, subunits. The second consists of the alpha-, beta'- and epsilon-COP, subunits. Here, we present the structure of the appendage domain of, gamma-COP and show that it has a similar overall fold as the, alpha-appendage of AP2. Again, like the alpha-appendage the gamma-COP, appendage possesses a single protein/protein interaction site on its, platform subdomain. We show that in yeast this site binds to the ARFGAP, Glo3p, and in mammalian gamma-COP this site binds to a Glo3p orthologue, ARFGAP2. On the basis of mutations in the yeast homologue of gamma-COP, Sec21p, a second binding site is proposed to exist on the gamma-COP, appendage that interacts with the alpha,beta',epsilon COPI subcomplex.
About this StructureAbout this Structure
1R4X is a Single protein structure of sequence from Homo sapiens with MG as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Gamma-COP appendage domain - structure and function., Watson PJ, Frigerio G, Collins BM, Duden R, Owen DJ, Traffic. 2004 Feb;5(2):79-88. PMID:14690497
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