Comparative phosphorylation kinetics of the human insulin receptor protein-tyrosine kinase domain and an enzymatically competent deletion construct - the tail could wag the dog

1995 ◽  
Vol 23 (2) ◽  
pp. 188S-188S ◽  
Author(s):  
PHILIP G. QUIRK ◽  
NOELEEN E. KEANE ◽  
BARRY A. LEVINE ◽  
LEI WEI ◽  
LELAND ELLIS
Keyword(s):  
Tyrosine Kinase ◽  
Insulin Receptor ◽  
Human Insulin ◽  
Protein Tyrosine Kinase ◽  
Kinase Domain ◽  
Receptor Protein ◽  
Tyrosine Kinase Domain ◽  
Human Insulin Receptor ◽  
Receptor Protein Tyrosine Kinase ◽  
Kinetics Of

N.m.r. structural studies on the tyrosine kinase domain of the human insulin receptor

1989 ◽  
Vol 17 (5) ◽  
pp. 899-899
Author(s):  
ROBERT A. ATKINSON ◽  
WAYNE J. FAIRBROTHER ◽  
BARRY A. LEVINE ◽  
JEREMY TAVARÈ ◽  
BEA CLACK ◽  
...  
Keyword(s):  
Tyrosine Kinase ◽  
Insulin Receptor ◽  
Human Insulin ◽  
Kinase Domain ◽  
Tyrosine Kinase Domain ◽  
Structural Studies ◽  
Human Insulin Receptor

Crystal structure of the tyrosine kinase domain of the human insulin receptor

Nature ◽  
1994 ◽  
Vol 372 (6508) ◽  
pp. 746-754 ◽  
Author(s):  
Stevan R. Hubbard ◽  
Lei Wei ◽  
Wayne A. Hendrickson
Keyword(s):  
Crystal Structure ◽  
Tyrosine Kinase ◽  
Insulin Receptor ◽  
Human Insulin ◽  
Kinase Domain ◽  
Tyrosine Kinase Domain ◽  
Human Insulin Receptor

scholarly journals Biochemical characterization of the protein tyrosine kinase homology domain of the ErbB3 (HER3) receptor protein

1997 ◽  
Vol 322 (3) ◽  
pp. 757-763 ◽  
Author(s):  
Susan L. SIERKE ◽  
Kunrong CHENG ◽  
Hong-Hee KIM ◽  
John G. KOLAND
Keyword(s):  
Tyrosine Kinase ◽  
Protein Tyrosine Kinase ◽  
Egf Receptor ◽  
Biochemical Characterization ◽  
Cd Spectroscopy ◽  
Receptor Protein ◽  
Tyrosine Kinase Domain ◽  
Protein Tyrosine ◽  
Receptor Protein Tyrosine Kinase ◽  
Her3 Receptor

The putative protein tyrosine kinase domain (TKD) of the ErbB3 (HER3) receptor protein was generated as a histidine-tagged recombinant protein (hisTKD-B3) and characterized enzymologically. CD spectroscopy indicated that the hisTKD-B3 protein assumed a native conformation with a secondary structure similar to that of the epidermal growth factor (EGF) receptor TKD. However, when compared with the EGF receptor-derived protein, hisTKD-B3 exhibited negligible intrinsic protein tyrosine kinase activity. Immune complex kinase assays of full-length ErbB3 proteins also yielded no evidence of catalytic activity. A fluorescence assay previously used to characterize the nucleotide-binding properties of the EGF receptor indicated that the ErbB3 protein was unable to bind nucleotide. The hisTKD-B3 protein was subsequently found to be an excellent substrate for the EGF receptor protein tyrosine kinase, which suggested that in vivophosphorylation of ErbB3 in response to EGF could be attributed to a direct cross-phosphorylation by the EGF receptor protein tyrosine kinase.

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