1r4x: Difference between revisions
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|PDB= 1r4x |SIZE=350|CAPTION= <scene name='initialview01'>1r4x</scene>, resolution 1.90Å | |PDB= 1r4x |SIZE=350|CAPTION= <scene name='initialview01'>1r4x</scene>, resolution 1.90Å | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM ION'>MG</scene> | |LIGAND= <scene name='pdbligand=CAS:S-(DIMETHYLARSENIC)CYSTEINE'>CAS</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1pzd|1PZD]], [[1b9k|1B9K]], [[1e42|1E42]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1r4x FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r4x OCA], [http://www.ebi.ac.uk/pdbsum/1r4x PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1r4x RCSB]</span> | |||
}} | }} | ||
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[[Category: Owen, D J.]] | [[Category: Owen, D J.]] | ||
[[Category: Watson, P J.]] | [[Category: Watson, P J.]] | ||
[[Category: | [[Category: adp-ribosylation factor]] | ||
[[Category: appendage | [[Category: appendage]] | ||
[[Category: beta sandwich]] | |||
[[Category: coatomer]] | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:23:20 2008'' | ||
Revision as of 23:23, 30 March 2008
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| , resolution 1.90Å | |||||||
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| Ligands: | , | ||||||
| Related: | 1PZD, 1B9K, 1E42
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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