THE SH3 DOMAIN OF EPS8 EXISTS AS A NOVEL INTERTWINED DIMER

File:1aoj.gif


1aoj, resolution 2.5Å

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OverviewOverview

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.

About this StructureAbout this Structure

1AOJ is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

ReferenceReference

The SH3 domain of Eps8 exists as a novel intertwined dimer., Kishan KV, Scita G, Wong WT, Di Fiore PP, Newcomer ME, Nat Struct Biol. 1997 Sep;4(9):739-43. PMID:9303002

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