Conformational change of Sos-derived proline-rich peptide upon binding Grb2 N-terminal SH3 domain probed by NMR


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Title:	Conformational change of Sos-derived proline-rich peptide upon binding Grb2 N-terminal SH3 domain probed by NMR
Authors:	Ogura, Kenji Browse this author →KAKEN DB
Authors:	Okamura, Hideyasu Browse this author
Issue Date:	9-Oct-2013
Publisher:	Nature publishing group
Journal Title:	Scientific reports
Volume:	3
Start Page:	2913
Publisher DOI:	10.1038/srep02913
PMID:	24105423
Abstract:	Growth factor receptor-bound protein 2 (Grb2) is a small adapter protein composed of a single SH2 domain flanked by two SH3 domains. The N-terminal SH3 (nSH3) domain of Grb2 binds a proline-rich region present in the guanine nucleotide releasing factor, son of sevenless (Sos). Using NMR relaxation dispersion and chemical shift analysis methods, we investigated the conformational change of the Sos-derived proline-rich peptide during the transition between the free and Grb2 nSH3-bound states. The chemical shift analysis revealed that the peptide does not present a fully random conformation but has a relatively rigid structure. The relaxation dispersion analysis detected conformational exchange of several residues of the peptide upon binding to Grb2 nSH3.
Rights:	http://creativecommons.org/licenses/by-nc-nd/3.0/
Type:	article
URI:	http://hdl.handle.net/2115/53623
Appears in Collections:	生命科学院・先端生命科学研究院 (Graduate School of Life Science / Faculty of Advanced Life Science) > 雑誌発表論文等 (Peer-reviewed Journal Articles, etc)

Submitter: 小椋賢治

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