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Structure of Rab GDP-dissociation inhibitor in complex with prenylated YPT1 GTPase.

Science (New York, N.Y.) | Oct 24, 2003

Rab/Ypt guanosine triphosphatases (GTPases) represent a family of key membrane traffic regulators in eukaryotic cells whose function is governed by the guanosine diphosphate (GDP) dissociation inhibitor (RabGDI). Using a combination of chemical synthesis and protein engineering, we generated and crystallized the monoprenylated Ypt1:RabGDI complex. The structure of the complex was solved to 1.5 angstrom resolution and provides a structural basis for the ability of RabGDI to inhibit the release of nucleotide by Rab proteins. Isoprenoid binding requires a conformational change that opens a cavity in the hydrophobic core of its domain II. Analysis of the structure provides a molecular basis for understanding a RabGDI mutant that causes mental retardation in humans.

Pubmed ID: 14576435 RIS Download

Mesh terms: Binding Sites | Crystallization | Crystallography, X-Ray | Guanine Nucleotide Dissociation Inhibitors | Guanosine Diphosphate | Hydrogen Bonding | Hydrophobic and Hydrophilic Interactions | Lipid Metabolism | Magnesium | Models, Molecular | Mutation | Protein Binding | Protein Conformation | Protein Prenylation | Protein Structure, Secondary | Protein Structure, Tertiary | Recombinant Proteins | Saccharomyces cerevisiae Proteins | rab GTP-Binding Proteins