2vwf | pdb_00002vwf

GRB2 SH3C (2)

spinqualitylabelsall models 2vwf, resolution 1.58Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2vwf is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 2h46, 1qg1, 1cj1, 1bm2, 1gfd, 1fyr, 1jyu, 1bmb, 1jyq, 1gfc, 2aob, 1x0n, 1tze, 1aze, 1gri, 2vvk, 1io6, 1fhs, 1zfp, 1gcq, 1ghu, 2aoa, 1jyr Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Grb2 and Gab2 form a complex implicated in normal cell signaling and cancer development. Binding of the Grb2SH3C domain to Gab2 is essential for the interaction, but molecular details remained undefined. Using peptide arrays and isothermal titration calorimetry, two Grb2SH3C binding sites in Gab2 (Gab2a and Gab2b) were confirmed and characterized. Gab2a bears similarity to a p27Kip1 epitope that also binds Grb2SH3C. Crystal structures of both Gab2 epitopes complexed with Grb2SH3C reveal that Gab2b contains a 3(10) helix that positions the arginine and lysine of the core-binding motif RxxK in parallel orientation. In contrast, the Gab2a RxxK motif is embedded in a PPII helix with Arg and Lys in staggered orientation. A similar interaction mode is also present in a new complex of Mona/GadsSH3C with an RxxxxK epitope from the putative phosphatase HD-PTP. In summary, our study reveals interaction types of SH3 domains, highlighting their great versatility. Distinct binding modes of two epitopes in Gab2 that interact with the SH3C domain of Grb2.,Harkiolaki M, Tsirka T, Lewitzky M, Simister PC, Joshi D, Bird LE, Jones EY, O'Reilly N, Feller SM Structure. 2009 Jun 10;17(6):809-22. PMID:19523899 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Growth factor receptor-bound protein

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