In vitro peptide binding to the heavy chain of the class I molecule of the major histocompatibility complex molecule HLA-A2.
The heavy chain of class I molecules of the major histocompatibility complex forms the binding site for antigenic peptides. We describe the binding of a synthetic peptide to the purified heavy chain of the human major histocompatibility complex molecule HLA-A2. The peptide binding capacity is found to be markedly increased if the protein is first partly denatured by reduction of its disulfide bonds in detergent and subsequently renatured by reoxidation. In the presence of certain detergents, the heavy chain binds peptides even when the protein is partly unfolded.
Dornmair
K
K
Stauffer Laboratory for Physical Chemistry, Stanford University, CA 94305.
Clark
B R
BR
McConnell
H M
HM
D000595:Amino Acid Sequence; D004591:Electrophoresis, Polyacrylamide Gel; D005456:Fluorescent Dyes; D015789:HLA-A2 Antigen / Q000276:immunology* / Q000302:isolation & purification; D015395:Histocompatibility Antigens Class I / Q000276:immunology; D006801:Humans; D046911:Macromolecular Substances; D008969:Molecular Sequence Data; D009975:Orthomyxoviridae; D010455:Peptides / Q000138:chemical synthesis; D011485:Protein Binding; D014763:Viral Matrix Proteins / Q000138:chemical synthesis
D005456:Fluorescent Dyes; D015789:HLA-A2 Antigen; D015395:Histocompatibility Antigens Class I; D046911:Macromolecular Substances; D010455:Peptides; D014763:Viral Matrix Proteins