1vg8: Difference between revisions
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[[Image:1vg8.jpg|left|200px]] | [[Image:1vg8.jpg|left|200px]] | ||
'''GPPNHP-Bound Rab7''' | {{Structure | ||
|PDB= 1vg8 |SIZE=350|CAPTION= <scene name='initialview01'>1vg8</scene>, resolution 1.70Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> and <scene name='pdbligand=GNP:PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER'>GNP</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''GPPNHP-Bound Rab7''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1VG8 is a [ | 1VG8 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=1VG8 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 14:45:10 2008'' | ||
Revision as of 12:45, 20 March 2008
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| 1vg8, resolution 1.70Å | |||||||||||||
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| Ligands: | MG and GNP | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
GPPNHP-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
1VG8 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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