v5.1.0.3
Glycine data from LIS
Type | Family |
Description | Rab proteins, a family of small Ras-related GTP-binding proteins, are involved in regulation of intracellular vesicle trafficking []. Rab GDP dissociation inhibitor (GDI) forms a soluble complex with Rab proteins, thereby preventing exchange of GDP for GTP. Rab GDI exists in several isoforms, and belongs to the TCD/MRS6 family of GDP dissociation inhibitors. The crystal structure of the bovine alpha-isoform of Rab GDI has been determined to a resolution of 1.81A []. The protein is composed of twomain structural units: a large complex multi-sheet domain I, and a smaller α-helical domain II.The structural organisation of domain I is closely related to FAD-containing monooxygenases and oxidases []. Conserved regions common to GDI and thechoroideraemia gene product, which delivers Rab to catalytic subunits of Rab geranylgeranyltransferase II, are clustered on one face of the domain[ ]. The two most conserved regions form a compact structure at the apex ofthe molecule; site-directed mutagenesis has shown these regions to play a critical role in the binding of Rab proteins []. |
Short Name | RabGDI |