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• W3046817657 startingPage "357" @default.
• W3046817657 abstract "The 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 Å resolution. The structure reveals antiparallel α-helices that associate through polar interactions. These include a remarkable stack of arginine residues within a four-helix bundle in the crystal lattice." @default.
• W3046817657 created "2020-08-07" @default.
• W3046817657 creator A5015057310 @default.
• W3046817657 creator A5039338285 @default.
• W3046817657 date "2020-07-28" @default.
• W3046817657 modified "2023-09-23" @default.
• W3046817657 title "Crystal structure of the Rab-binding domain of Rab11 family-interacting protein 2" @default.
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• W3046817657 doi "https://doi.org/10.1107/s2053230x20009164" @default.
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• W3046817657 hasPublicationYear "2020" @default.
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