Importance of peptide amino and carboxyl termini to the stability of MHC class I molecules.
An influenza virus matrix peptide in which either the charged amino or carboxyl terminus was substituted by methyl groups promoted folding of the class I human histocompatibility antigen (HLA-A2). A peptide modified at both termini did not promote stable folding. The thermal stability of HLA-A2 complexed with peptides that did not have either terminus was approximately 22 degrees C lower than that of the control peptide, whereas matrix peptide in which both anchor positions were substituted by alanines had its stability decreased by only 5.5 degrees C. Thus, the conserved major histocompatibility complex class I residues at both ends of the peptide binding site form energetically important sites for binding the termini of short peptides.
Department of Biochemistry and Molecular Biology, Harvard University, Cambridge, MA 02138.
M
M
Bouvier
D C
DC
Wiley
D000595:Amino Acid Sequence; D001665:Binding Sites; D015789:HLA-A2 Antigen / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D006801:Humans; D006860:Hydrogen Bonding; D008969:Molecular Sequence Data; D009154:Mutation; D009975:Orthomyxoviridae; D010455:Peptides / Q000737:chemistry* / Q000378:metabolism; D011489:Protein Denaturation; D017510:Protein Folding; D013696:Temperature; D013816:Thermodynamics; D013820:Thermolysin / Q000737:chemistry; D014763:Viral Matrix Proteins / Q000737:chemistry* / Q000378:metabolism; D001613:beta 2-Microglobulin / Q000737:chemistry
D015789:HLA-A2 Antigen; D010455:Peptides; D014763:Viral Matrix Proteins; D001613:beta 2-Microglobulin; D013820:Thermolysin