1r4x
From Proteopedia
(New page: 200px<br /> <applet load="1r4x" size="450" color="white" frame="true" align="right" spinBox="true" caption="1r4x, resolution 1.90Å" /> '''Crystal Structure A...) |
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caption="1r4x, resolution 1.90Å" /> | caption="1r4x, resolution 1.90Å" /> | ||
'''Crystal Structure Analys of the Gamma-COPI Appendage domain'''<br /> | '''Crystal Structure Analys of the Gamma-COPI Appendage domain'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1R4X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MG as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1R4X is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MG:'>MG</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R4X OCA]. |
==Reference== | ==Reference== | ||
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[[Category: appendage; beta sandwich; coatomer; adp-ribosylation factors]] | [[Category: appendage; beta sandwich; coatomer; adp-ribosylation factors]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:46:55 2008'' |
Revision as of 14:46, 15 February 2008
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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 with as ligand. 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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