Conformational effect of phosphorylation on T cell receptor/CD3 zeta-chain sequences.

Abstract:

: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.

authors

Laczkó I,Hollósi M,Vass E,Hegedüs Z,Monostori E,Tóth GK

doi

10.1006/bbrc.1997.7989

subject

Has Abstract

pub_date

1998-01-26 00:00:00

pages

474-9

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006291X97979894

journal_volume

242

pub_type

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