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A TIRF Microscopy Technique for Real-time, Simultaneous Imaging of the TCR and its Associated Signaling Proteins
Published on: March 22, 2012
Conformational effect of phosphorylation on T cell receptor/CD3 zeta-chain sequences
1Institute of Biophysics, Biological Research Center, Szeged, Hungary. laczko@everx.szbk.u-szeged.hu
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.
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