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

The SH3 domain of Eps8 exists as a novel intertwined dimer.
type: AcademicArticle
type: Article
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
volume: 4
issue: 9
is part of: Nature structural biology
status: peerReviewed
status: published
author list: authors
type: EPrint
type: ArticleEPrint
is part of: repository
subject: QR Microbiology

NPG
type: Organization

Nature structural biology
type: Collection
issn: 10728368

G Scita
type: Person
given name: G
family name: Scita

M E Newcomer
type: Person
given name: M E
family name: Newcomer

W T Wong
type: Person
given name: W T
family name: Wong

P P Di Fiore
type: Person
given name: P P
family name: Di Fiore

K V Radha Kishan
type: Person
given name: K V Radha
family name: Kishan

HTML Summary of #771 The SH3 domain of Eps8 exists as a novel intertwined dimer.
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primary topic: The SH3 domain of Eps8 exists as a novel intertwined dimer.

QR Microbiology
type: Concept