1aoj

THE SH3 DOMAIN OF EPS8 EXISTS AS A NOVEL INTERTWINED DIMER

spinqualitylabelsall models 1aoj, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1aoj is a 2 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.5Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function EPS8_MOUSE Upon binding to EGF receptor/EGFR enhances EGF-dependent mitogenic signals. Can bind multiple cellular targets. 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 SH3 domains are structurally well-characterized as monomeric modular units of protein structure that mediate protein-protein recognition in numerous signal transduction proteins. The X-ray crystallographic structure of the Eps8 SH3 domain reveals a novel variation of the canonical SH3 fold: the SH3 domain from Eps8 is a dimer formed by strand interchange. In addition, co-immunoprecipitation experiments show that intact Eps8 is multimeric in vivo. Hence, the SH3 domain of Eps8 may represent a dimerization motif. The SH3 domain of Eps8 exists as a novel intertwined dimer.,Kishan KV, Scita G, Wong WT, Di Fiore PP, Newcomer ME Nat Struct Biol. 1997 Sep;4(9):739-43. PMID:9303002 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Epidermal growth factor receptor substrate 3D structures

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