1vg0
From Proteopedia
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'''The crystal structures of the REP-1 protein in complex with monoprenylated Rab7 protein''' | '''The crystal structures of the REP-1 protein in complex with monoprenylated Rab7 protein''' | ||
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[[Category: Pylypenko, O.]] | [[Category: Pylypenko, O.]] | ||
[[Category: Rak, A.]] | [[Category: Rak, A.]] | ||
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| - | [[Category: | + | [[Category: Rab prenylation]] |
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Revision as of 09:29, 3 May 2008
The crystal structures of the REP-1 protein in complex with monoprenylated 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
1VG0 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 Page seeded by OCA on Sat May 3 12:29:56 2008
