PubMed:10728873 JSONTXT

{"project":"IAV-Glycan_IAV_human_2","denotations":[{"id":"T1","span":{"begin":330,"end":338},"obj":"subtype"},{"id":"T2","span":{"begin":339,"end":341},"obj":"H1"},{"id":"T3","span":{"begin":343,"end":345},"obj":"H2"},{"id":"T4","span":{"begin":350,"end":352},"obj":"H3"},{"id":"T5","span":{"begin":586,"end":599},"obj":"substitution"},{"id":"T6","span":{"begin":620,"end":627},"obj":"subtype"},{"id":"T7","span":{"begin":843,"end":845},"obj":"H1"},{"id":"T8","span":{"begin":932,"end":934},"obj":"H2"},{"id":"T9","span":{"begin":939,"end":941},"obj":"H3"}],"text":"Effect of chain length on the conformation and T cell recognition of synthetic hemagglutinin fragments.\nCircular dichroism and Fourier-transform infrared spectroscopies were used to compare the conformational mobility of 13-mer peptides covering the 317-329 region of the envelope protein hemagglutinin of human influenza A virus subtypes H1, H2 and H3 with that of their truncated deca- and nonapeptide analogs. These peptides were demonstrated to bind to the murine I-Ed major histocompatibility complex encoded class II and human HLA-B*2705 class I molecules. Despite the amino acid substitutions in the three 13-mer subtype sequences, no significant differences in the conformational properties could be shown. Deletion of the N-terminal three residues resulted in a shift to an increased alpha-helical conformer population in the 317-329 H1 peptide and the breakage of the 3(10) or weakly H-bonded (nascent) alpha-helix in the H2 and H3 peptides. The conformational change observed upon deletion did not influence the efficiency of I-Ed peptide interaction, however, the C-terminal Arg had a beneficial effect both on MHC class II and class I binding without causing any remarkable change in solution conformation."}