1lv0

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(New page: 200px<br /><applet load="1lv0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lv0, resolution 2.00&Aring;" /> '''Crystal structure of...)
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Revision as of 18:47, 20 November 2007

Image:1lv0.jpg

1lv0, resolution 2.00Å

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Crystal structure of the Rab effector guanine nucleotide dissociation inhibitor (GDI) in complex with a geranylgeranyl (GG) peptide

Overview

Rab GTPases, key regulators of membrane targeting and fusion, require the, covalent attachment of geranylgeranyl lipids to their C terminus for, function. To elucidate the role of lipid in Rab recycling, we have, determined the crystal structure of Rab guanine nucleotide dissociation, inhibitor (alphaGDI) in complex with a geranylgeranyl (GG) ligand, (H(2)N-Cys-(S-GG)-OMe). The lipid is bound beneath the Rab binding, platform in a shallow hydrophobic groove. Mutation of the binding pocket, in the brain-specific alphaGDI leads to mental retardation. Strikingly, lipid binding acts through a conserved allosteric switching mechanism to, promote release of the GDI-Rab[GDP] complex from the membrane.

About this Structure

1LV0 is a Single protein structure of sequence from Bos taurus with SO4 and GER as ligands. Full crystallographic information is available from OCA.

Reference

Geranylgeranyl switching regulates GDI-Rab GTPase recycling., An Y, Shao Y, Alory C, Matteson J, Sakisaka T, Chen W, Gibbs RA, Wilson IA, Balch WE, Structure. 2003 Mar;11(3):347-57. PMID:12623022

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