The foreign antigen binding site and T cell recognition regions of class I histocompatibility antigens
- 1 October 1987
- journal article
- Published by Springer Science and Business Media LLC in Nature
- Vol. 329 (6139), 512-518
- https://doi.org/10.1038/329512a0
Abstract
Most of the polymorphic amino acids of the class I histocompatibility antigen, HLA-A2, are clustered on top of the molecule in a large groove identified as the recognition site for processed foreign antigens. Many residues critical for T-cell recognition of HLA are located in this site, in positions allowing them to serve as ligands to processed antigens. These findings have implications for how the products of the major histocompatibility complex (MHC) recognize foreign antigens.This publication has 49 references indexed in Scilit:
- In vitro mutagenesis at a single residue introduces B and T cell epitopes into a class I HLA molecule.The Journal of Experimental Medicine, 1987
- Interaction of peptide antigens and class II major histocompatibility complex antigensNature, 1986
- Speculations on Sequence Homologies between the fibronectin cell-attachment site, major histocompatibility antigens, and a putative AIDS virus polypeptideHuman Immunology, 1986
- The epitopes of influenza nucleoprotein recognized by cytotoxic T lymphocytes can be defined with short synthetic peptidesCell, 1986
- Binding of immunogenic peptides to Ia histocompatibility moleculesNature, 1985
- Identical Vβ T-cell receptor genes used in alloreactive cytotoxic and antigen plus I–A specific helper T cellsNature, 1985
- The class II molecules of the human and murine major histocompatibility complexCell, 1984
- Antigen recognition by H-2-restricted T cells. I. Cell-free antigen processing.The Journal of Experimental Medicine, 1983
- Restriction of in vitro T cell-mediated cytotoxicity in lymphocytic choriomeningitis within a syngeneic or semiallogeneic systemNature, 1974
- GENETIC CONTROL OF THE ANTIBODY RESPONSE IN INBRED MICEThe Journal of Experimental Medicine, 1968