Structural highlights
Function
EPS8_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 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[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Fazioli F, Minichiello L, Matoska V, Castagnino P, Miki T, Wong WT, Di Fiore PP. Eps8, a substrate for the epidermal growth factor receptor kinase, enhances EGF-dependent mitogenic signals. EMBO J. 1993 Oct;12(10):3799-808. PMID:8404850
- ↑ Kishan KV, Scita G, Wong WT, Di Fiore PP, Newcomer ME. The SH3 domain of Eps8 exists as a novel intertwined dimer. Nat Struct Biol. 1997 Sep;4(9):739-43. PMID:9303002
