6S8X
Crystal structure of the Rab-binding domain of FIP2
Summary for 6S8X
| Entry DOI | 10.2210/pdb6s8x/pdb |
| Descriptor | Rab11 family-interacting protein 2, HEXANE-1,6-DIOL (3 entities in total) |
| Functional Keywords | membrane trafficking, rab small gtpases, effector protein, rab-binding domain, endosomal trafficking, signaling protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 4 |
| Total formula weight | 36603.43 |
| Authors | Kearney, A.M.,Khan, A.R. (deposition date: 2019-07-10, release date: 2020-08-05, Last modification date: 2024-05-15) |
| Primary citation | Kearney, A.M.,Khan, A.R. Crystal structure of the Rab-binding domain of Rab11 family-interacting protein 2. Acta Crystallogr.,Sect.F, 76:357-363, 2020 Cited by PubMed 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. PubMed: 32744247DOI: 10.1107/S2053230X20009164 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.29 Å) |
Structure validation
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