2MBG

Rlip76 (gap-gbd)

Summary for 2MBG

• Entry DOI: 10.2210/pdb2mbg/pdb
• NMR Information: BMRB: 17608
• Descriptor: RalA-binding protein 1 (1 entity in total)
• Functional Keywords: rhogap, ralbp1, protein binding
• Biological source: Homo sapiens (human)
• Cellular location: Membrane; Peripheral membrane protein: Q15311
• Total number of polymer chains: 1
• Total formula weight: 31015.14

Authors

Rajasekar, K.V.,Campbell, L.J.,Nietlispach, D.,Owen, D.,Mott, H.R. (deposition date: 2013-07-30, release date: 2013-12-04, Last modification date: 2024-05-15)

Primary citation

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

Experimental method

SOLUTION NMR