1vg1
From Proteopedia
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| - | [[Image:1vg1.jpg|left|200px]] | + | [[Image:1vg1.jpg|left|200px]] |
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| - | '''GDP-Bound Rab7''' | + | {{Structure |
| + | |PDB= 1vg1 |SIZE=350|CAPTION= <scene name='initialview01'>1vg1</scene>, resolution 1.90Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=GDP:GUANOSINE-5'-DIPHOSPHATE'>GDP</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''GDP-Bound Rab7''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1VG1 is a [ | + | 1VG1 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VG1 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/15186776 15186776] |
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: gtp-binding protein]] | [[Category: gtp-binding protein]] | ||
| - | ''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 14:45:04 2008'' |
Revision as of 12:45, 20 March 2008
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| , resolution 1.90Å | |||||||
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| Ligands: | and | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
GDP-Bound Rab7
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
1VG1 is a Single protein structure of sequence 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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