The SH3 domain of Eps8 exists as a novel intertwined dimer
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.
Publication Source (Journal or Book title)
Nature Structural Biology
Radha Kishan, K., Scita, G., Wong, W., Fiore, P., & Newcomer, M. (1997). The SH3 domain of Eps8 exists as a novel intertwined dimer. Nature Structural Biology, 4 (9), 739-743. https://doi.org/10.1038/nsb0997-739