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1vg9

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(New page: 200px<br /><applet load="1vg9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vg9, resolution 2.50&Aring;" /> '''The crystal structur...)
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Revision as of 02:41, 21 November 2007

Image:1vg9.jpg

1vg9, resolution 2.50Å

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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 with MG, K, GDP and P33 as ligands. 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 Wed Nov 21 04:49:13 2007

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