Rab-binding domain
IPR010911
Definition
This entry represents the Rab-binding domain. 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 PMID:12578829. The crystal structure of the Rab effector domain of Rabphilin-3A in complex with Rab3A has been solved PMID:10025402. The structure consists of two long helices separated by an atypical FYVE-type zinc finger which adopts a conformation similar to classical ones. 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.
12 human proteins with this domain
Each is a reviewed human protein in the Seroatlas serome and a potential autoantibody target; this domain groups them into one antibody-relevant category. Every entry links to its own record.
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