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.
Mesh Terms:
Adaptor Proteins, Signal Transducing, Amino Acid Sequence, Animals, COS Cells, Crystallography, X-Ray, Cytoskeletal Proteins, Dimerization, Mice, Models, Molecular, Molecular Sequence Data, Precipitin Tests, Protein Conformation, Proteins, Recombinant Fusion Proteins, Sequence Alignment, src Homology Domains
Adaptor Proteins, Signal Transducing, Amino Acid Sequence, Animals, COS Cells, Crystallography, X-Ray, Cytoskeletal Proteins, Dimerization, Mice, Models, Molecular, Molecular Sequence Data, Precipitin Tests, Protein Conformation, Proteins, Recombinant Fusion Proteins, Sequence Alignment, src Homology Domains
Nat. Struct. Biol.
Date: Sep. 01, 1997
PubMed ID: 9303002
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