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

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

doi:10.1038/nsb1294-891

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

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

Research output: Contribution to journal › Article › peer-review

101 Citations (Scopus)

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 Abl, Fyn and p85.

Original language	English
Pages (from-to)	891-997
Number of pages	107
Journal	Nature Structural Biology
Volume	1
Issue number	12
DOIs	https://doi.org/10.1038/nsb1294-891
Publication status	Published - Dec 1994
Externally published	Yes

All Science Journal Classification (ASJC) codes

Structural Biology
Biochemistry
Genetics

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

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 Abl, Fyn and p85.",

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",

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doi = "10.1038/nsb1294-891",

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T1 - Structure of the N-terminal SH3 domain of GRB2 complexed with a peptide from the guanine nucleotide releasing factor Sos

AU - Terasawa, Hiroaki

AU - Kohda, Daisuke

AU - Hatanaka, Hideki

AU - Tsuchiya, Shigeo

AU - Ogura, Kenji

AU - Nagata, Koji

AU - Ishii, Shunsuke

AU - Mandiyan, Valsan

AU - Ullrich, Axel

AU - Schlessinger, Joseph

AU - Inagaki, Fuyuhiko

PY - 1994/12

Y1 - 1994/12

N2 - 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 Abl, Fyn and p85.

AB - 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 Abl, Fyn and p85.

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

Abstract

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