title: Identification of a ten-amino acid proline-rich SH3 binding site.
abstract: The Src homology 3 (SH3) region is a small protein domain present in a very large group of proteins, including cytoskeletal elements and signaling proteins. It is believed that SH3 domains serve as modules that mediate protein-protein associations and, along with Src homology 2 (SH2) domains, regulate cytoplasmic signaling. The SH3 binding sites of two SH3 binding proteins were localized to a nine- or ten-amino acid stretch very rich in proline residues. Similar SH3 binding motifs exist in the formins, proteins that function in pattern formation in embryonic limbs of the mouse, and one subtype of the muscarinic acetylcholine receptor. Identification of the SH3 binding site provides a basis for understanding the interaction between the SH3 domains and their targets.
authors.affiliation: Rockefeller University, New York, NY 10021.
authors.forename: R
authors.initials: R
authors.lastname: Ren
authors.forename: B J
authors.initials: BJ
authors.lastname: Mayer
authors.forename: P
authors.initials: P
authors.lastname: Cicchetti
authors.forename: D
authors.initials: D
authors.lastname: Baltimore
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D003598:Cytoskeletal Proteins / Q000235:genetics / Q000378:metabolism*; D004247:DNA / Q000235:genetics / Q000378:metabolism; D016313:Genes, abl; D005982:Glutathione Transferase / Q000235:genetics / Q000378:metabolism; D007700:Kinetics; D051379:Mice; D008969:Molecular Sequence Data; D011392:Proline; D016315:Proto-Oncogene Proteins c-abl / Q000235:genetics / Q000378:metabolism*; D051381:Rats; D011976:Receptors, Muscarinic / Q000378:metabolism; D011993:Recombinant Fusion Proteins / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D015398:Signal Transduction
chemical_list: D003598:Cytoskeletal Proteins; D011976:Receptors, Muscarinic; D011993:Recombinant Fusion Proteins; D004247:DNA; D011392:Proline; D005982:Glutathione Transferase; D016315:Proto-Oncogene Proteins c-abl