title: The SH3 domain of Eps8 exists as a novel intertwined dimer.
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.
authors.affiliation: Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, TN 37232-0146, USA.
authors.forename: K V
authors.initials: KV
authors.lastname: Kishan
authors.forename: G
authors.initials: G
authors.lastname: Scita
authors.forename: W T
authors.initials: WT
authors.lastname: Wong
authors.forename: P P
authors.initials: PP
authors.lastname: Di Fiore
authors.forename: M E
authors.initials: ME
authors.lastname: Newcomer
mesh_terms: 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
chemical_list: D048868:Adaptor Proteins, Signal Transducing; D003598:Cytoskeletal Proteins; C083430:Eps8 protein, mouse; D011506:Proteins; D011993:Recombinant Fusion Proteins