Ontology type: schema:ScholarlyArticle
1994-12-01
AUTHORSHiroaki Terasawa, Daisuke Kohda, Hideki Hatanaka, Shigeo Tsuchiya, Kenji Ogura, Koji Nagata, Shunsuke Ishii, Valsan Mandiyan, Axel Ullrich, Joseph Schlessinger, Fuyuhiko Inagaki
ABSTRACTSrc-homology 3 (SH3) domains mediate signal transduction by binding to proline-rich motifs in target proteins. We have determined the high-resolution NMR structure of the complex between the amino-terminal SH3 domain of GRB2 and a ten amino acid peptide derived from the guanine nucleotide releasing factor Sos. The NMR data show that the peptide adopts the conformation of a left-handed polyproline type II helix and interacts with three major sites on the SH3 domain. The orientation of the bound peptide is opposite to that of proline-rich peptides bound to the SH3 domains of AbI, Fyn and p85. More... »
PAGES891-897
http://scigraph.springernature.com/pub.10.1038/nsb1294-891
DOIhttp://dx.doi.org/10.1038/nsb1294-891
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PUBMEDhttps://www.ncbi.nlm.nih.gov/pubmed/7773778
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