6s8x | pdb_00006s8x
Crystal structure of the Rab-binding domain of FIP2
Structural highlights
Function[RFIP2_HUMAN] A Rab11 effector protein acting in the regulation of the transport of vesicles from the endosomal recycling compartment (ERC) to the plasma membrane. Also involved in receptor-mediated endocytosis and membrane trafficking of recycling endosomes, probably originating from clathrin-coated vesicles. Binds preferentially to phosphatidylinositol 3,4,5-trisphosphate (PtdInsP3) and phosphatidic acid (PA). Required in a complex with MYO5B and RAB11 for the transport of NPC1L1 to the plasma membrane. Also acts as a regulator of cell polarity.[1] [2] [3] [4] Publication Abstract from PubMedThe small GTPases Rab11, Rab14 and Rab25 regulate membrane trafficking through the recruitment of Rab11 family-interacting proteins (FIPs) to endocytic compartments. FIPs are multi-domain effector proteins that have a highly conserved Rab-binding domain (RBD) at their C-termini. Several structures of complexes of Rab11 with RBDs have previously been determined, including those of Rab11-FIP2 and Rab11-FIP3. In addition, the structures of the Rab14-FIP1 and Rab25-FIP2 complexes have been determined. All of the RBD structures contain a central parallel coiled coil in the RBD that binds to the switch 1 and switch 2 regions of the Rab. Here, the crystal structure of the uncomplexed RBD of FIP2 is presented at 2.3 A resolution. The structure reveals antiparallel alpha-helices that associate through polar interactions. These include a remarkable stack of arginine residues within a four-helix bundle in the crystal lattice. Crystal structure of the Rab-binding domain of Rab11 family-interacting protein 2.,Kearney AM, Khan AR Acta Crystallogr F Struct Biol Commun. 2020 Aug 1;76(Pt 8):357-363. doi:, 10.1107/S2053230X20009164. Epub 2020 Jul 28. PMID:32744247[5] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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