The SH3 domain of Eps8 exists as a novel intertwined dimer.

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

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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.

Item Type: Article
Additional Information: Copyright of this article belongs to NPG.
Subjects: Q Science > QR Microbiology
Depositing User: Dr. K.P.S.Sengar
Date Deposited: 27 Jan 2012 14:58
Last Modified: 10 Apr 2012 11:35
URI: http://crdd.osdd.net/open/id/eprint/771

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