| Literature DB >> 9464240 |
I Laczkó1, M Hollósi, E Vass, Z Hegedüs, E Monostori, G K Tóth.
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.Entities:
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Year: 1998 PMID: 9464240 DOI: 10.1006/bbrc.1997.7989
Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN: 0006-291X Impact factor: 3.575