creators_name: Kishan, K V Radha
creators_name: Scita, G
creators_name: Wong, W T
creators_name: Di Fiore, P P
creators_name: Newcomer, M E
type: article
datestamp: 2012-01-27 14:58:03
lastmod: 2012-04-10 11:35:15
metadata_visibility: show
title: The SH3 domain of Eps8 exists as a novel intertwined dimer.
ispublished: pub
subjects: QR
full_text_status: none
note: Copyright of this article belongs to NPG.
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.
date: 1997-09
date_type: published
publication: Nature structural biology
volume: 4
number: 9
publisher: NPG
pagerange: 739-43
refereed: TRUE
issn: 1072-8368
citation:   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