Conformational analysis of the phosphorylated epidermal growth factor receptor.
Phosphorylation-induced conformational changes have been well documented with different receptor tyrosine kinases. However. the susceptible epitopes and the tyrosine residue(s) involved in particular structural alteration mostly remain to be determined. Using a conformation-specific anti-peptide antibody, we have not only identified one such domain in the C-terminal tail of the EGF receptor but also identified the phosphate acceptor sites that are involved in the conformational change.
Bishayee
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Department of Pathology and Laboratory Medicine, UMDNJ-New Jersey Medical School, Newark 07103-2714, USA.
Beguinot
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Bishayee
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S
D016475:3T3 Cells; D019943:Amino Acid Substitution; D000596:Amino Acids / Q000737:chemistry / Q000378:metabolism; D000818:Animals; D001665:Binding Sites; D066246:ErbB Receptors / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D051379:Mice; D008954:Models, Biological; D010766:Phosphorylation; D011233:Precipitin Tests; D011487:Protein Conformation
D000596:Amino Acids; D066246:ErbB Receptors