Conformational effect of phosphorylation on T cell receptor CD3 ζ-chain sequences

被引：28

作者：

Laczkó, I

Hollósi, M

Vass, E

Hegedus, Z

Monostori, E

Tóth, GK

机构：

[1] Biol Res Ctr, Inst Biophys, H-6701 Szeged, Hungary

[2] Biol Res Ctr, Genet Inst, H-6701 Szeged, Hungary

[3] Eotvos Lorand Univ, Dept Organ Chem, H-1518 Budapest 112, Hungary

[4] Albert Szent Gyorgyi Med Univ, Dept Med Chem, H-6720 Szeged 8, Hungary

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1998年 / 242卷 / 03期

基金：

匈牙利科学研究基金会;

关键词：

D O I：

10.1006/bbrc.1997.7989

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：

The effect of tyrosine-phosphorylation on the conformation of three tyrosine-based immunoreceptor activation motifs, zeta(69-86), zeta(106-126), and zeta(138-155), located in the T cell receptor/CD3 zeta-chain was investigated. Circular dichroism and Fourier-transform infrared spectroscopy of the nonphosphorylated and phosphorylated fragments gave evidence that phosphorylation can alter the secondary structure of the peptides. The most significant - alpha-helix to beta-sheet -conformational change was observed in the case of the zeta(138-155) peptide sequence which may be relevant to recognition by Src homology 2 (SH2) domains of signaling proteins. (C) 1998 Academic Press.

引用

页码：474 / 479

页数：6

共 25 条

[1] EXAMINATION OF THE SECONDARY STRUCTURE OF PROTEINS BY DECONVOLVED FTIR SPECTRA [J].