Analysis of Substrate Recognition Determinants in a Synthetic Peptide Containing the Tyr 1173 Autophosphorylation Site of the Epidermal Growth Factor Receptor

1995 ◽  
Vol 316 (2) ◽  
pp. 745-750 ◽  
Author(s):  
C.K. Klingbeil ◽  
G.N. Gill ◽  
D.L. Cadena
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Synthetic Peptide ◽  
Substrate Recognition ◽  
Growth Factor Receptor ◽  
Epidermal Growth ◽  
Autophosphorylation Site

scholarly journals Conversion of a phosphoseryl/threonyl phosphatase into a phosphotyrosyl phosphatase

1988 ◽  
Vol 256 (3) ◽  
pp. 1029-1034 ◽  
Author(s):  
J Goris ◽  
C J Pallen ◽  
P J Parker ◽  
J Hermann ◽  
M D Waterfield ◽  
...  
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Phosphatase Activity ◽  
Growth Factor Receptor ◽  
Xenopus Laevis Oocytes ◽  
Rous Sarcoma ◽  
Sarcoma Virus ◽  
Epidermal Growth ◽  
Autophosphorylation Site

By use of the autophosphorylated epidermal-growth-factor receptor and the synthetic peptide RRLIE-DAEY(P)AARG, representing an autophosphorylation site of the transforming protein of Rous-sarcoma virus, it is demonstrated that the phosphotyrosyl phosphatase activity of the polycation-stimulated phosphatases is substantially increased by an enzyme-directed effect of ATP or PPi. Concomitant with this increase in phosphotyrosyl phosphatase activity, the phosphorylase phosphatase activity is decreased, thus dramatically changing the substrate specificity of these enzymes. The dephosphorylation of four different phosphotyrosyl sites of the epidermal-growth-factor receptor is neither consecutive nor at random, but a preferred dephosphorylation of the P1 site over the P3 greater than P2 greater than P4 sites is observed. This phosphatase activity represents a substantial fraction of the total phosphotyrosyl phosphatase activity in the post-mitochondrial supernatant of Xenopus laevis oocytes.

Investigation of a synthetic peptide as immunogen for a variant epidermal growth factor receptor associated with gliomas

1993 ◽  
Vol 46 (1-2) ◽  
pp. 165-173 ◽  
Author(s):  
Carol J. Wikstrand ◽  
S.David Stanley ◽  
Peter A. Humphrey ◽  
Charles N. Pegram ◽  
Gerald E. Archer ◽  
...  
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Synthetic Peptide ◽  
Growth Factor Receptor ◽  
Epidermal Growth

scholarly journals Identification of a novel autophosphorylation site (P4) on the epidermal growth factor receptor

1989 ◽  
Vol 262 (2) ◽  
pp. 659-663 ◽  
Author(s):  
J J Hsuan ◽  
N Totty ◽  
M D Waterfield
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Tryptic Peptide ◽  
Growth Factor Receptor ◽  
Intact Cells ◽  
C Terminus ◽  
Partial Digestion ◽  
Epidermal Growth ◽  
Autophosphorylation Site

Three major autophosphorylation sites are located near the C-terminus of the epidermal growth factor receptor, but a fourth site is repeatedly detected. We report here the purification and sequencing of a tryptic peptide containing this site, Tyr-1086. Furthermore, we demonstrate that additional phosphopeptides are observed following both partial digestion and overdigestion. Finally, we show that Tyr-1086 can be phosphorylated in intact cells.

scholarly journals Computational delineation of tyrosyl-substrate recognition and catalytic landscapes by the epidermal growth factor receptor tyrosine kinase domain

2014 ◽  
Vol 10 (7) ◽  
pp. 1890-1904
Author(s):  
Yingting Liu ◽  
Ravi Radhakrishnan
Keyword(s):  
Epidermal Growth Factor Receptor ◽  
Growth Factor ◽  
Epidermal Growth Factor ◽  
Tyrosine Kinase ◽  
Substrate Recognition ◽  
Growth Factor Receptor ◽  
Kinase Domain ◽  
Tyrosine Kinase Domain ◽  
Phosphoryl Transfer ◽  
Epidermal Growth

Computational delineation of the binding modes of tyrosyl substrate recognition by the epidermal growth factor receptor (EGFR) tyrosine kinase domain (TKD) and subsequent phosphoryl transfer.

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