1vg9
From Proteopedia
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|PDB= 1vg9 |SIZE=350|CAPTION= <scene name='initialview01'>1vg9</scene>, resolution 2.50Å | |PDB= 1vg9 |SIZE=350|CAPTION= <scene name='initialview01'>1vg9</scene>, resolution 2.50Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=GDP:GUANOSINE-5'-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=P33:3,6,9,12,15,18-HEXAOXAICOSANE-1,20-DIOL'>P33</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1ltx|1LTX]], [[1vg0|1VG0]], [[1vg1|1VG1]], [[1vg8|1VG8]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vg9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vg9 OCA], [http://www.ebi.ac.uk/pdbsum/1vg9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1vg9 RCSB]</span> | ||
}} | }} | ||
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[[Category: Pylypenko, O.]] | [[Category: Pylypenko, O.]] | ||
[[Category: Rak, A.]] | [[Category: Rak, A.]] | ||
| - | [[Category: GDP]] | ||
| - | [[Category: K]] | ||
| - | [[Category: MG]] | ||
| - | [[Category: P33]] | ||
[[Category: post-translational modification]] | [[Category: post-translational modification]] | ||
[[Category: rab prenylation]] | [[Category: rab prenylation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:24:08 2008'' |
Revision as of 21:24, 30 March 2008
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| , resolution 2.50Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , , | ||||||
| Related: | 1LTX, 1VG0, 1VG1, 1VG8
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
The crystal structures of the REP-1 protein in complex with C-terminally truncated Rab7 protein
Overview
Members of the RabGDI/REP family serve as multifunctional regulators of the Rab family of GTP binding proteins. Mutations in members of this family, such as REP-1, lead to abnormalities, including progressive retinal degradation (choroideremia) in humans. The crystal structures of the REP-1 protein in complex with monoprenylated or C-terminally truncated Rab7 proteins revealed that Rab7 interacts with the Rab binding platform of REP-1 via an extended interface involving the Switch 1 and 2 regions. The C terminus of the REP-1 molecule functions as a mobile lid covering a conserved hydrophobic patch on the surface of REP-1 that in the complex coordinates the C terminus of Rab proteins. Using semisynthetic fluorescent Rab27A, we demonstrate that although Rab27A can be prenylated by REP-2, this reaction can be effectively inhibited by other Rab proteins, providing a possible explanation for the accumulation of unprenylated Rab27A in choroideremia.
About this Structure
1VG9 is a Protein complex structure of sequences from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Structure of the Rab7:REP-1 complex: insights into the mechanism of Rab prenylation and choroideremia disease., Rak A, Pylypenko O, Niculae A, Pyatkov K, Goody RS, Alexandrov K, Cell. 2004 Jun 11;117(6):749-60. PMID:15186776
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