The SH3 domain of Eps8 exists as a novel intertwined dimer

K. Y. Radha Kishan, Giorgio Scita, William T. Wong, Pier Paolo Di Fiore, Marcia E. Newcomer

Research output: Contribution to journalArticle

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.

Original languageEnglish
Pages (from-to)739-743
Number of pages5
JournalNature Structural Biology
Volume4
Issue number9
DOIs
Publication statusPublished - 1997

ASJC Scopus subject areas

  • Biochemistry
  • Structural Biology
  • Genetics

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    Radha Kishan, K. Y., Scita, G., Wong, W. T., Fiore, P. P. D., & Newcomer, M. E. (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