%0 Journal Article
%@ 1072-8368
%A Kishan, K V Radha
%A Scita, G
%A Wong, W T
%A Di Fiore, P P
%A Newcomer, M E
%D 1997
%F open:771
%I NPG
%J Nature structural biology
%N 9
%P 739-43
%T The SH3 domain of Eps8 exists as a novel intertwined dimer.
%U http://crdd.osdd.net/open/771/
%V 4
%X 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.
%Z Copyright of this article belongs to NPG.