IPR000806
Rab GDI protein
InterPro entry
Short name | RabGDI |
Overlapping homologous superfamilies | |
family relationships |
Description
Rab proteins, a family of small Ras-related GTP-binding proteins, are involved in regulation of intracellular vesicle trafficking
[1]. 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
[2]. The protein is composed of two main 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
[2]. Conserved regions common to GDI and the choroideraemia gene product, which delivers Rab to catalytic subunits of Rab geranylgeranyltransferase II, are clustered on one face of the domain
[1]. The two most conserved regions form a compact structure at the apex of the molecule; site-directed mutagenesis has shown these regions to play a critical role in the binding of Rab proteins
[2].
References
1.Cloning of a brain-type isoform of human Rab GDI and its expression in human neuroblastoma cell lines and tumor specimens. Nishimura N, Goji J, Nakamura H, Orita S, Takai Y, Sano K. Cancer Res. 55, 5445-50, (1995). View articlePMID: 7585614
2.Structure and mutational analysis of Rab GDP-dissociation inhibitor. Schalk I, Zeng K, Wu SK, Stura EA, Matteson J, Huang M, Tandon A, Wilson IA, Balch WE. Nature 381, 42-8, (1996). View articlePMID: 8609986
GO terms
biological process
molecular function
cellular component
- None
Contributing Member Database Entry
- PRINTS:PR00892