The SH3 Domain of Eps8 Exists As a Novel Intertwined Dimer

Overview

Journal Nat Struct Biol

Specialty Cell Biology

Date 1997 Sep 26

PMID 9303002

Citations 24

Authors

K V Kishan

G Scita

W T Wong

P P Di Fiore

M E Newcomer

Affiliations

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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.

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