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| {{STRUCTURE_1r4x| PDB=1r4x | SCENE= }} | | {{STRUCTURE_1r4x| PDB=1r4x | SCENE= }} |
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| '''Crystal Structure Analys of the Gamma-COPI Appendage domain'''
| | ===Crystal Structure Analys of the Gamma-COPI Appendage domain=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_14690497}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 14690497 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_14690497}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Beta sandwich]] | | [[Category: Beta sandwich]] |
| [[Category: Coatomer]] | | [[Category: Coatomer]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:04:48 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 08:49:38 2008'' |