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The SH3 domain of Eps8 exists as a novel intertwined dimer

Nature Structural Biology volume 4, pages 739–743 (1997)Cite this article

Abstract

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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Authors and Affiliations

  1. Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN, 37232-0146, USA

    K.V. Radha Kishan

  2. Department of Experimental Oncology, European Institute of Oncology, Milan, Italy

    Giorgio Scita

  3. Laboratory of Cellular Development and Oncology, National Institute of Dental Research, National Institutes of Health, Bethesda, MD, 20892, USA

    William T. Wong

  4. Department of Experimental Oncology, European Institute of Oncology, Milan, Italy

    Pier Paolo Di Fiore

  5. Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN, 37232-0146, USA

    Marcia E. Newcomer

  6. Istituto di Microbiologia, Facolta di Medicina e Chirurgia, Bari, Italy

    Pier Paolo Di Fiore & Marcia E. Newcomer

Authors
  1. K.V. Radha Kishan
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  2. Giorgio Scita
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  3. William T. Wong
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  4. Pier Paolo Di Fiore
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  5. Marcia E. Newcomer
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Radha Kishan, K., Scita, G., Wong, W. et al. The SH3 domain of Eps8 exists as a novel intertwined dimer. Nat Struct Mol Biol 4, 739–743 (1997). https://doi.org/10.1038/nsb0997-739

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