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Title
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The SH3 domain of Eps8 exists as a novel intertwined dimer.
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Authors
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K.V.Kishan,
G.Scita,
W.T.Wong,
P.P.Di Fiore,
M.E.Newcomer.
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Ref.
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Nat Struct Biol, 1997,
4,
739-743.
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PubMed id
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Abstract
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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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