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From Proteopedia
THE SH3 DOMAIN OF EPS8 EXISTS AS A NOVEL INTERTWINED DIMER
Structural highlights
FunctionEPS8_MOUSE Upon binding to EGF receptor/EGFR enhances EGF-dependent mitogenic signals. Can bind multiple cellular targets.[1] 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 PubMedSH3 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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