2KWH
Ral binding domain of RLIP76 (RalBP1)
Summary for 2KWH
| Entry DOI | 10.2210/pdb2kwh/pdb |
| Related | 2KWI |
| NMR Information | BMRB: 15524 |
| Descriptor | RalA-binding protein 1 (1 entity in total) |
| Functional Keywords | gtpase activation, transport protein |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 1 |
| Total formula weight | 6600.57 |
| Authors | Fenwick, R.B.,Campbell, L.J.,Rajasekar, K.,Prasannan, S.,Nietlispach, D.,Camonis, J.,Owen, D.,Mott, H.R. (deposition date: 2010-04-12, release date: 2010-09-01, Last modification date: 2024-05-15) |
| Primary citation | Fenwick, R.B.,Campbell, L.J.,Rajasekar, K.,Prasannan, S.,Nietlispach, D.,Camonis, J.,Owen, D.,Mott, H.R. The RalB-RLIP76 complex reveals a novel mode of ral-effector interaction Structure, 18:985-995, 2010 Cited by PubMed Abstract: RLIP76 (RalBP1) is a multidomain protein that interacts with multiple small G protein families: Ral via a specific binding domain, and Rho and R-Ras via a GTPase activating domain. RLIP76 interacts with endocytosis proteins and has also been shown to behave as a membrane ATPase that transports chemotherapeutic agents from the cell. We have determined the structure of the Ral-binding domain of RLIP76 and show that it comprises a coiled-coil motif. The structure of the RLIP76-RalB complex reveals a novel mode of binding compared to the structures of RalA complexed with the exocyst components Sec5 and Exo84. RLIP76 interacts with both nucleotide-sensitive regions of RalB, and key residues in the interface have been identified using affinity measurements of RalB mutants. Sec5, Exo84, and RLIP76 bind Ral proteins competitively and with similar affinities in vitro. PubMed: 20696399DOI: 10.1016/j.str.2010.05.013 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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