Abstract
SH2 and SH3 domains are elements that control interactions of cytoplasmic signaling proteins. SH2 is a structural domain to bind to phosphotyrosine containing sequences, while SH3 binds to proline rich peptide sequences. Grb2 is an adaptor protein containing a SH2 domain flanked by two SH3 domains. Grb2 mediates signals from growth factor receptors to Ras. This pathway is recognized as a major signal transduction pathway for cell proliferation and differentiation. In addition, Grb2 plays important roles for controlling cytoskeletons in response to extracellular sitimuli. Grb2 is now regarded as a prototype of adaptor proteins and its structural studies complexed with target peptides gave basic clues for the molecular mechanism of target recognition by SH2 and SH3 domains. We started to determine the structures of the complexes of the individual SH2 and SH3 domains of Grb2 and the target peptides by NMR and X-ray crystallography in order to elucidate the molecular mechanism for canonical and non-canonical target recognition.
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Inagaki, F. (2003). Structural Biology of Signal Transduction Mediated by Grb2. In: Yagasaki, K., Miura, Y., Hatori, M., Nomura, Y. (eds) Animal Cell Technology: Basic & Applied Aspects. Animal Cell Technology: Basic & Applied Aspects, vol 13. Springer, Dordrecht. https://doi.org/10.1007/978-94-017-0726-8_8
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DOI: https://doi.org/10.1007/978-94-017-0726-8_8
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