1lfd
From Proteopedia
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CRYSTAL STRUCTURE OF THE ACTIVE RAS PROTEIN COMPLEXED WITH THE RAS-INTERACTING DOMAIN OF RALGDS
Contents |
Overview
The Ras protein signals to a number of distinct pathways by interacting, with diverse downstream effectors. Among the effectors of Ras are the Raf, kinase and RalGDS, a guanine nucleotide dissociation stimulator specific, for Ral. Despite the absence of significant sequence similarities, both, effectors bind directly to Ras, but with different specificities. We, report here the 2.1 A crystal structure of the complex between Ras and the, Ras-interacting domain (RID) of RalGDS. This structure reveals that the, beta-sheet of the RID joins the switch I region of Ras to form an extended, beta-sheet with a topology similar to that found in the Rap-Raf complex., However, the side chain interactions at the joining junctions of the two, interacting systems and the relative orientation of the two binding, domains are distinctly different. Furthermore, in the case of the Ras-RID, complex a second RID molecule also interacts with a different part of the, Ras molecule, the switch II region. These findings account for the, cross-talk between the Ras and Ral pathways and the specificity with which, Ras distinguishes the two effectors.
Disease
Known diseases associated with this structure: Bladder cancer, somatic OMIM:[190020], Costello syndrome OMIM:[190020], Thyroid carcinoma, follicular, somatic OMIM:[190020]
About this Structure
1LFD is a Protein complex structure of sequences from Homo sapiens and Rattus norvegicus with MG and GNP as ligands. Full crystallographic information is available from OCA.
Reference
Structural basis for the interaction of Ras with RalGDS., Huang L, Hofer F, Martin GS, Kim SH, Nat Struct Biol. 1998 Jun;5(6):422-6. PMID:9628477
Page seeded by OCA on Mon Nov 12 17:59:42 2007
