Nature Structural Biology
4, 739 - 743 (1997)
doi:10.1038/nsb0997-739
The SH3 domain of Eps8 exists as a novel intertwined dimerK.V. Radha Kishan1, Giorgio Scita2, William T. Wong3, Pier Paolo Di Fiore4
& Marcia E. Newcomer5, 6
1Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN 37232-0146, USA.
2Department of Experimental Oncology, European Institute of Oncology, Milan, Italy.
3Laboratory of Cellular Development and Oncology, National Institute of Dental Research, National Institutes of Health, Bethesda, MD 20892, USA.
4Department of Experimental Oncology, European Institute of Oncology, Milan, Italy and Istituto di Microbiologia, Facolta di Medicina e Chirurgia, Bari, Italy
5Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN 37232-0146, USA.
6newmmer@lhmrba.hh.vanderbilt.edu 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.
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