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

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Abstract

The effect of tyrosine-phosphorylation on the conformation of three tyrosine-based immunoreceptor activation motifs, ζ(69-86), ζ(106-126), and ζ(138-155), located in the T cell receptor/CD3 ζ-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 - α-helix to β-sheet - conformational change was observed in the case of the ζ(138-155) peptide sequence which may be relevant to recognition by Src homology 2 (SH2) domains of signaling proteins.

Original languageEnglish
Pages (from-to)474-479
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume242
Issue number3
DOIs
Publication statusPublished - Jan 26 1998

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Phosphorylation
T-Cell Antigen Receptor
Tyrosine
Immunoreceptor Tyrosine-Based Activation Motif
Peptides
src Homology Domains
Fourier Transform Infrared Spectroscopy
Circular Dichroism
Conformations
Chemical activation
Proteins

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

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abstract = "The effect of tyrosine-phosphorylation on the conformation of three tyrosine-based immunoreceptor activation motifs, ζ(69-86), ζ(106-126), and ζ(138-155), located in the T cell receptor/CD3 ζ-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 - α-helix to β-sheet - conformational change was observed in the case of the ζ(138-155) peptide sequence which may be relevant to recognition by Src homology 2 (SH2) domains of signaling proteins.",
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T1 - Conformational effect of phosphorylation on T cell receptor/CD3 ζ-chain sequences

AU - Laczkó, I.

AU - Hollósi, M.

AU - Vass, E.

AU - Hegedűs, Z.

AU - Monostori, E.

AU - Tóth, G.

PY - 1998/1/26

Y1 - 1998/1/26

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AB - The effect of tyrosine-phosphorylation on the conformation of three tyrosine-based immunoreceptor activation motifs, ζ(69-86), ζ(106-126), and ζ(138-155), located in the T cell receptor/CD3 ζ-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 - α-helix to β-sheet - conformational change was observed in the case of the ζ(138-155) peptide sequence which may be relevant to recognition by Src homology 2 (SH2) domains of signaling proteins.

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