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Structure of the Rab7:REP-1 complex: insights into the mechanism of Rab prenylation and choroideremia disease.

Authors: Rak, A  Pylypenko, O  Niculae, A  Pyatkov, K  Goody, RS  Alexandrov, K 
Citation: Rak A, etal., Cell. 2004 Jun 11;117(6):749-60.
Pubmed: (View Article at PubMed) PMID:15186776
DOI: Full-text: DOI:10.1016/j.cell.2004.05.017

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.

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CRRD Object Information
CRRD ID: 8553294
Created: 2014-05-08
Species: All species
Last Modified: 2014-05-08
Status: ACTIVE



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