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High structural side chain specificity required at the second position of immunogenic peptides to obtain stable MHC/peptide complexes
Author(s) -
Gavioli Riccardo,
Guerrini Remo,
Masucci Maria Grazia,
Tomatis Roberto,
Traniello Serena,
Marastoni Mauro
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(97)01540-8
Subject(s) - peptide , residue (chemistry) , chemistry , side chain , stereochemistry , amino acid , stereospecificity , lysine , peptide sequence , biochemistry , polymer , organic chemistry , gene , catalysis
Peptides binding to HLA‐A11 contain a hydrophobic or a small polar amino acid at position 2 and a lysine at the carboxy terminus. Synthetic peptides carrying natural and unnatural amino acids in position 2 were used to determine the requirements for formation of stable HLA‐A11/peptide complexes. By kinetic analysis we demonstrate that a stereospecific interaction between the side chain residue in position 2 and a subsite of pocket B is required to obtain stable HLA/peptide complexes. This specific interaction is mediated by a methyl group or by an ethyl group bound to the asymmetric C β atom with the correct configuration. Experiments performed with different peptide sequences suggest that the presence of adequate anchor residues may be sufficient to produce stable HLA/peptide complexes.