Peptide-induced conformational changes in class I heavy chains alter major histocompatibility complex recognition.
Small peptides, derived from endogenous proteins bind within the antigen binding groove created by the beta-pleated sheets and alpha helices of the alpha 1 and alpha 2 domains of the class I molecule of the major histocompatibility complex (MHC). However, the precise role of peptide in class I MHC conformation remains unclear. Here, we have shown that, in at least some instances, changes induced in the MHC molecule by the binding of distinct peptides can be identified as specific alterations in serological epitopes expressed on the class I protein. The nature of specific peptides expressed by class I-bearing cells may, therefore, have a dramatic influence on T cell development, self-tolerance, and alloreactivity.
Bluestone
J A
JA
Department of Pathology, Ben May Institute, University of Chicago, Illinois 60637.
Jameson
S
S
Miller
S
S
Dick
R
R
D000595:Amino Acid Sequence; D000818:Animals; D000911:Antibodies, Monoclonal; D001665:Binding Sites; D002472:Cell Transformation, Viral; D015395:Histocompatibility Antigens Class I / Q000737:chemistry* / Q000378:metabolism; D006801:Humans; D008223:Lymphoma; D008285:Major Histocompatibility Complex; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D010047:Ovalbumin / Q000737:chemistry / Q000276:immunology; D010455:Peptides / Q000138:chemical synthesis / Q000737:chemistry*; D011487:Protein Conformation; D011925:Rauscher Virus / Q000235:genetics; D014407:Tumor Cells, Cultured
D000911:Antibodies, Monoclonal; D015395:Histocompatibility Antigens Class I; D010455:Peptides; D010047:Ovalbumin