Assignment of backbone 1H, 13C, and 15N resonances of the SH2 domain of human Grb14.
The (1)H, (13)C, and (15)N backbone resonance assignments have been made for the Src homology 2 (SH2) domain of the human molecular adapter protein Grb14. The assignments, along with the majority of the non-aromatic side-chain (1)H and (13)C resonances are reported. The SH2 domain has been complexed with a phosphotyrosine-containing peptide (pY766) corresponding to the putative binding site in the fibroblast growth factor receptor (FGFR1). Chemical shift changes upon binding are also reported.
Scharf
Paul J
PJ
Department of Biochemistry, College of Medicine, University of Vermont, Burlington 05405, USA.
Lyons
Barbara A
BA
D048868:Adaptor Proteins, Signal Transducing; D002247:Carbon Isotopes; D006801:Humans; D006859:Hydrogen; D009587:Nitrogen Isotopes; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods*; D011506:Proteins / Q000737:chemistry*; D018909:src Homology Domains
D048868:Adaptor Proteins, Signal Transducing; D002247:Carbon Isotopes; C099655:GRB14 protein, human; D009587:Nitrogen Isotopes; D011506:Proteins; D006859:Hydrogen