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

@article{Terasawa1994StructureOT,
  title={Structure of the N-terminal SH3 domain of GRB2 complexed with a peptide from the guanine nucleotide releasing factor Sos},
  author={Hiroaki Terasawa and Daisuke Kohda and Hideki Hatanaka and Shigeo Tsuchiya and Kenji Ogura and Koji Nagata and Shunsuke Ishii and Valsan Mandiyan and Axel Ullrich and Joseph Schlessinger and Fuyuhiko Inagaki},
  journal={Nature Structural Biology},
  year={1994},
  volume={1},
  pages={891-897}
}
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… CONTINUE READING

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