The SH3 domain of Eps8 exists as a novel intertwined dimer.
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.
Kishan
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Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN 37232-0146, USA.
Scita
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Wong
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Di Fiore
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Newcomer
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D048868:Adaptor Proteins, Signal Transducing; D000595:Amino Acid Sequence; D000818:Animals; D019556:COS Cells; D018360:Crystallography, X-Ray; D003598:Cytoskeletal Proteins; D019281:Dimerization; D051379:Mice; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011233:Precipitin Tests; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry* / Q000235:genetics; D011993:Recombinant Fusion Proteins; D016415:Sequence Alignment; D018909:src Homology Domains
D048868:Adaptor Proteins, Signal Transducing; D003598:Cytoskeletal Proteins; C083430:Eps8 protein, mouse; D011506:Proteins; D011993:Recombinant Fusion Proteins