|PROSITE documentation PDOC50916 [for PROSITE entry PS50916]|
Rab are small GTPases implicated in vesicle trafficking. Like the other small GTPases, Rab proteins act as molecular switches, with an active GTP-bound form that interacts with its target or effector protein and an inactive GDP-bound form. A subgroup of Rab effectors contain in their N-terminal part a conserved region of around 70 amino acid residues, the Rab-binding domain (RabBD) . In some Rab effector domains an atypical FYVE-type zinc finger is inserted in the central part .
The crystal structure of the Rab effector domain of Rabphilin-3A in complex with Rab3A has been solved  (see <PDB:1ZBD>). The structure consists of two long helices separated by an atypical FYVE-type zinc finger which adopts a conformation similar to classical ones (see <PDOC50178>). The central zinc finger does not directly interact with Rab3A. The amino acids important for this interaction are located around a short C-terminal motif (SGAWFF) and an acidic cluster in the N-terminal area.
Proteins known to contain a Rab-binding domain are listed below:
The profile we developed covers the entire Rab-binding domain.Last update:
July 2003 / First entry.
PROSITE method (with tools and information) covered by this documentation:
|Title||Distinct Rab binding specificity of Rim1, Rim2, rabphilin, and Noc2. Identification of a critical determinant of Rab3A/Rab27A recognition by Rim2.|
|Source||J. Biol. Chem. 278:15373-15380(2003).|
|2||Authors||Ostermeier C. Brunger A.T.|
|Title||Structural basis of Rab effector specificity: crystal structure of the small G protein Rab3A complexed with the effector domain of rabphilin-3A.|