Structure of the N-terminal SH3 domain of GRB2 complexed with a peptide from the guanine nucleotide releasing factor Sos View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1994-12-01

AUTHORS

Hiroaki Terasawa, Daisuke Kohda, Hideki Hatanaka, Shigeo Tsuchiya, Kenji Ogura, Koji Nagata, Shunsuke Ishii, Valsan Mandiyan, Axel Ullrich, Joseph Schlessinger, Fuyuhiko Inagaki

ABSTRACT

Src-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... »

PAGES

891-897

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/nsb1294-891

DOI

http://dx.doi.org/10.1038/nsb1294-891

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1017171313

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/7773778


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