Structure of the N-terminal SH3 domain of GRB2 complexed with a peptide from the guanine nucleotide releasing factor Sos
作者： Hiroaki Terasawa , Daisuke Kohda , Hideki Hatanaka , Shigeo Tsuchiya , Kenji Ogura
DOI: 10.1038/NSB1294-891
关键词:
摘要: 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 complex between amino-terminal SH3 domain GRB2 and a ten amino acid peptide derived from guanine nucleotide releasing factor Sos. The data show that adopts conformation left-handed polyproline type II helix interacts with three major sites on domain. orientation bound is opposite peptides AbI, Fyn p85.
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