Literature DB >> 9303002

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

K V Kishan1, G Scita, W T Wong, P P Di Fiore, M E Newcomer.   

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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Year:  1997        PMID： 9303002     DOI： 10.1038/nsb0997-739

Source DB:  PubMed          Journal:  Nat Struct Biol        ISSN： 1072-8368


  22 in total

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5.  Computational studies of the reversible domain swapping of p13suc1.

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7.  Structural insights into the recognition of β3 integrin cytoplasmic tail by the SH3 domain of Src kinase.

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8.  EPS8 upregulates FOXM1 expression, enhancing cell growth and motility.

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9.  Effect of pH and salt bridges on structural assembly: molecular structures of the monomer and intertwined dimer of the Eps8 SH3 domain.

Authors:  K V Kishan; M E Newcomer; T H Rhodes; S D Guilliot
Journal:  Protein Sci       Date:  2001-05       Impact factor: 6.725

10.  Molecular basis for the dual function of Eps8 on actin dynamics: bundling and capping.

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Journal:  PLoS Biol       Date:  2010-06-01       Impact factor: 8.029
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