title: The SH3 domain of Eps8 exists as a novel intertwined dimer.
creator: Kishan, K V Radha
creator: Scita, G
creator: Wong, W T
creator: Di Fiore, P P
creator: Newcomer, M E
subject: QR Microbiology
description: 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.
publisher: NPG
date: 1997-09
type: Article
type: PeerReviewed
identifier:   Kishan, K V Radha and Scita, G and Wong, W T and Di Fiore, P P and Newcomer, M E  (1997) The SH3 domain of Eps8 exists as a novel intertwined dimer.  Nature structural biology, 4 (9).  pp. 739-43.  ISSN 1072-8368     
relation: http://crdd.osdd.net/open/771/