Open AccessIn vitro peptide binding to the heavy chain of the class I molecule of the major histocompatibility complex molecule HLA-A2.
Author(s) -
Klaus Dornmair,
Brian R. Clark,
Harden M. McConnell
Publication year - 1991
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.88.4.1335
Subject(s) - peptide , major histocompatibility complex , human leukocyte antigen , chemistry , histocompatibility , biochemistry , in vitro , plasma protein binding , binding site , immunoglobulin light chain , molecule , biology , antigen , antibody , genetics , gene , organic chemistry
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.