Conformational analysis of the phosphorylated epidermal growth factor receptor

被引：4

作者：

Bishayee, A

Beguinot, L

Bishayee, S

机构：

[1] Univ Med & Dent New Jersey, New Jersey Med Sch, Dept Pathol & Lab Med, Newark, NJ 07103 USA

[2] CNR, Inst Neurosci & Bioimaging, I-20132 Milan, Italy

[3] DIBIT, Mol Oncol Unit, I-20132 Milan, Italy

来源：

BIOSCIENCE REPORTS | 1999年 / 19卷 / 05期

关键词：

antigenic determinant; autophosphorylation sites; conformation-specific antibody; EGF receptor; receptor tyrosine kinase;

D O I：

10.1023/A:1020260105524

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：397 / 402

页数：6

共 13 条

[1] Phosphorylation of tyrosine 992, 1068, and 1086 is required for conformational change of the human epidermal growth factor receptor C-terminal tail [J].