2MBG

Rlip76 (gap-gbd)

2MBG の概要

• エントリーDOI: 10.2210/pdb2mbg/pdb
• NMR情報: BMRB: 17608
• 分子名称: RalA-binding protein 1 (1 entity in total)
• 機能のキーワード: rhogap, ralbp1, protein binding
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Membrane; Peripheral membrane protein: Q15311
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 31015.14

構造登録者

Rajasekar, K.V.,Campbell, L.J.,Nietlispach, D.,Owen, D.,Mott, H.R. (登録日: 2013-07-30, 公開日: 2013-12-04, 最終更新日: 2024-05-15)

主引用文献

Rajasekar, K.V.,Campbell, L.J.,Nietlispach, D.,Owen, D.,Mott, H.R.
The Structure of the RLIP76 RhoGAP-Ral Binding Domain Dyad: Fixed Position of the Domains Leads to Dual Engagement of Small G Proteins at the Membrane.
Structure, 21:2131-2142, 2013

PubMed Abstract: RLIP76 is an effector for Ral small GTPases, which in turn lie downstream of the master regulator Ras. Evidence is growing that Ral and RLIP76 play a role in tumorigenesis, invasion, and metastasis. RLIP76 contains both a RhoGAP domain and a Ral binding domain (GBD) and is, therefore, a node between Ras and Rho family signaling. The structure of the RhoGAP-GBD dyad reveals that the RLIP76 RhoGAP domain adopts a canonical RhoGAP domain structure and that the linker between the two RLIP76 domains is structured, fixing the orientation of the two domains and allowing RLIP76 to interact with Rho-family GTPases and Ral simultaneously. However, the juxtaposed domains do not influence each other functionally, suggesting that the RLIP76-Ral interaction controls cellular localization and that the fixed orientation of the two domains orientates the RhoGAP domain with respect to the membrane, allowing it to be perfectly poised to engage its target G proteins.

PubMed: 24207123
DOI: 10.1016/j.str.2013.09.007

実験手法

SOLUTION NMR