Conformational Effect of Phosphorylation on T Cell Receptor/CD3 ζ-Chain Sequences

• Published in: Biochemical and biophysical research communications Vol. 242; no. 3; pp. 474 - 479
• Main Authors: Laczkó, Ilona, Hollósi, Miklós, Vass, Elemér, Hegedűs, Zoltán, Monostori, Éva, Tóth, Gábor K.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 26.01.1998
• Subjects: Amino Acid Sequence; CD3 Complex - chemistry; Circular Dichroism; Molecular Sequence Data; Peptide Fragments - chemical synthesis; Phosphorylation; Phosphotyrosine - metabolism; Protein Conformation; Protein Structure, Secondary; Receptors, Antigen, T-Cell - chemistry; Spectroscopy, Fourier Transform Infrared; src Homology Domains - physiology
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1006/bbrc.1997.7989

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.