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Protein Science (2004), 13:2541-2546. Published by Cold Spring Harbor Laboratory Press. Copyright © 2004 The Protein Society
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PROTEIN STRUCTURE REPORT

Solution structure of the human Grb14–SH2 domain and comparison with the structures of the human Grb7–SH2/erbB2 peptide complex and human Grb10–SH2 domain

Paul J. Scharf1, Jill Witney2,3, Roger Daly2 and Barbara A. Lyons1

1 Department of Biochemistry, College of Medicine, University of Vermont, Burlington, Vermont 05405, USA
2 Garvan Institute of Medical Research, St. Vincent’s Hospital, Sydney, NSW 2010, Australia

(RECEIVED May 26, 2004; FINAL REVISION June 7, 2004; ACCEPTED June 8, 2004)

Grb14 is an adapter protein that is known to be overexpressed in estrogen receptor positive breast cancers, and in a number of prostate cancer cell lines. Grb14 has been demonstrated to bind to a number of activated receptor tyrosine kinases (RTKs) and to modulate signals transduced through these receptors. The RTKs to which Grb14 binds include the insulin receptor (IR), the fibroblast growth factor receptor (FGFR), the platelet-derived growth factor receptor (PDGFR), and the tunica endothelial kinase (Tek/Tie2) receptor. Grb14 has been shown to bind to these activated RTKs through its Src homology 2 (SH2) domain, with the exception of the insulin receptor, where the primary binding interaction is via a small domain adjacent to the SH2 domain (the BPS or PIR domain). Grb14 is a member of the Grb7 family of proteins, which also includes Grb7 and Grb10. We have solved the solution structure of the human Grb14–SH2 domain and compared it with the recently determined Grb7–SH2 and Grb10–SH2 domain structures.

Keywords: Src homology 2; nuclear magnetic resonance; cell signaling; protein structure

Abbreviations: BPS, "between plekstrin and Src" • EGFR, epidermal growth factor receptor • erbB2 (a.k.a. HER2, EGFR2), Erythroblastosis B • FGFR, fibroblast growth factor receptor • Grb, growth factor receptor bound • HSQC, heteronuclear single-quantum coherence • IR, insulin receptor • NMR, nuclear magnetic resonance • NOE, nuclear Overhauser effect • NOESY, NOE spectroscopy • PDGFR, platelet-derived growth factor receptor • TEK, tunica endothelial kinase • RMSD, root-mean-square deviation • RTK, receptor tyrosine kinase • SH2, Src homology 2

Article and publication are at http://www.proteinscience.org/cgi/doi/10.1110/ps.04884704.

Reprint requests to: Barbara A. Lyons, Department of Biochemistry, C415, Given Medical Building, 89 Beaumont Avenue, Burlington, VT 05405, USA; e-mail: Barbara.Lyons{at}uvm.edu; fax: (802) 862-8229.


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