Solution Structure of the SH2 Domain of Grb2/Ash Complexed with EGF Receptor-Derived Phosphotyrosine-Containing Peptide.
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概要
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1H, 13C, and 15N NMR resonances of the SH2 domain of Grb2/Ash in both the free form and the form complexed with a phosphotyrosine-containing peptide derived from the EGF receptor were assigned by analysis of multi-dimensional, double- and triple-resonance NMR experiments. From the chemical shift changes of individual residues upon peptide binding, the binding site for the peptide was mapped on the structure of Grb2/Ash SH2. The peptide was not recognized by the groove formed by the BG and EF loops, suggesting that the EGFR peptide does not bind to Grb2/Ash SH2 in an extended conformation. This was supported by analysis of the binding affinity of mutants where residues on the BG and EF loops were changed to alanine. The present results are consistent with the recently reported structures of Grb2/Ash SH2 complexed with BCR-Abl and Shc-derived phosphotyrosine containing peptides, where the peptide forms a turn conformation. This shows that the specific conformation of the phosphotyrosine-containing sequence is required for the SH2 binding responsible for downstream signaling.
- 社団法人 日本生化学会の論文
著者
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OGURA Kenji
Department of Molecular Physiology, Tokyo Metropolitan Institute of Medical Science
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Mandiyan Valsan
Department Of Pharmacology New York University Medical Center
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Ohta Hiromichi
Department Of Applied Chemistry School Of Engineering Nagoya University
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Tsuchiya Shigeo
Department Of Anesthesiology Sapporo Medical University School Of Medicine
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Schlessinger Joseph
Department Of Pharmacology New York University Medical Center
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Nagata Koji
Department Of Applied Biological Chemistry Graduate School Of Agricultural And Life Sciences The Uni
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Terasawa Hiroaki
Department Of Chemistry Tokyo Institute Of Technology
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Aimoto Saburo
Protein Research Institute Osaka University
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Ogura Kenji
Department Of Molecular Physiology Tokyo Metropolitan Institute Of Medical Science
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Inagaki Fuyuhiko
Department of Biophysics and Biochemistry, Faculty of Science, The University of Tokyo
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Hatanaka Hideki
Department of Molecular Physiology, The Tokyo Metropolitan Institute of Medical Science
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