2KWH

Ral binding domain of RLIP76 (RalBP1)

2KWH の概要

• エントリーDOI: 10.2210/pdb2kwh/pdb
• 関連するPDBエントリー: 2KWI
• NMR情報: BMRB: 15524
• 分子名称: RalA-binding protein 1 (1 entity in total)
• 機能のキーワード: gtpase activation, transport protein
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 6600.57

構造登録者

Fenwick, R.B.,Campbell, L.J.,Rajasekar, K.,Prasannan, S.,Nietlispach, D.,Camonis, J.,Owen, D.,Mott, H.R. (登録日: 2010-04-12, 公開日: 2010-09-01, 最終更新日: 2024-05-15)

主引用文献

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

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: 20696399
DOI: 10.1016/j.str.2010.05.013

実験手法

SOLUTION NMR