1r4x
From Proteopedia
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| - | [[Image:1r4x.jpg|left|200px]] | + | [[Image:1r4x.jpg|left|200px]] |
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| - | '''Crystal Structure Analys of the Gamma-COPI Appendage domain''' | + | {{Structure |
| + | |PDB= 1r4x |SIZE=350|CAPTION= <scene name='initialview01'>1r4x</scene>, resolution 1.90Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Crystal Structure Analys of the Gamma-COPI Appendage domain''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1R4X is a [ | + | 1R4X is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R4X OCA]. |
==Reference== | ==Reference== | ||
| - | 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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/14690497 14690497] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: Watson, P J.]] | [[Category: Watson, P J.]] | ||
[[Category: MG]] | [[Category: MG]] | ||
| - | [[Category: appendage; beta sandwich; coatomer; adp-ribosylation | + | [[Category: appendage; beta sandwich; coatomer; adp-ribosylation factor]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:46:53 2008'' |
Revision as of 11:46, 20 March 2008
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| , resolution 1.90Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal Structure Analys of the Gamma-COPI Appendage domain
Overview
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 Structure
1R4X is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
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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