@article{open771,
          volume = {4},
          number = {9},
           month = {September},
          author = {K V Radha Kishan and G Scita and W T Wong and P P Di Fiore and M E Newcomer},
            note = {Copyright of this article belongs to NPG.},
           title = {The SH3 domain of Eps8 exists as a novel intertwined dimer.},
       publisher = {NPG},
            year = {1997},
         journal = {Nature structural biology},
           pages = {739--43},
             url = {http://crdd.osdd.net/open/771/},
        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.}
}