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The SH3 domain of Eps8 exists as a novel intertwined dimer

Nature Structural Biology volume 4, pages 739743 (1997) | Download Citation

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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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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 and Istituto di Microbiologia, Facolta di Medicina e Chirurgia, Bari, Italy

    • Pier Paolo Di Fiore
  5. Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN 37232-0146, USA.

    • Marcia E. Newcomer
  6. newmmer@lhmrba.hh.vanderbilt.edu

    • Marcia E. Newcomer

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DOI

https://doi.org/10.1038/nsb0997-739

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