A synthetic peptide termed core peptide (CP), which corresponds to a specific sequence of the TCR-α chain transmembrane domain, is known to inhibit IL-2 production in antigen stimulated T-cells. The molecular mechanism of the TCR inhibition is not known. This study examined the effects of CP on TCR subunit assembly and TCR cell surface expression in vitro. Co-transfection experiments between TCR-α and CD3-δ using COS-7 cells, and the interaction between TCR- and the CD3 proteins in a T-cell line (2B4) were analysed after incubation with CP or its conjugates. Results indicate that CP co-precipitates with CD3-δ and CD3-η in vitro, without any effect on TCR-α /CD3-δ dimerisation or TCR multisubunit assembly and cell surface expression.
Department of Rheumatology,Westmead Hospital, Westmead, NSW 2145, Australia.
Publication date: March 1, 2007
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Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.