Identification of self peptides bound to purified HLA-B27
- 1 September 1991
- journal article
- research article
- Published by Springer Science and Business Media LLC in Nature
- Vol. 353 (6342), 326-329
- https://doi.org/10.1038/353326a0
Abstract
A pool of endogenous peptides bound to the human class I MHC molecule, HLA-B27, has been isolated. Microsequence analysis of the pool and of 11 HPLC-purified peptides provides information on the binding specificity of the HLA-B27 molecule. The peptides all seem to be nonamers, seven of which match to protein sequences in a database search. These self peptides derive from abundant cytosolic or nuclear proteins, such as histone, ribosomal proteins, and members of the 90K heat-shock protein family.Keywords
This publication has 43 references indexed in Scilit:
- The structure of HLA-B27 reveals nonamer self-peptides bound in an extended conformationNature, 1991
- Assembly of MHC class I molecules analyzed in vitroCell, 1990
- Developmental Biology of T Cells in T Cell-Receptor Transgenic MiceAnnual Review of Immunology, 1990
- Specificity pockets for the side chains of peptide antigens in HLA-Aw68Nature, 1989
- Association of class I major histocompatibility heavy and light chains induced by viral peptidesNature, 1989
- Developmental Biology of T Cell ReceptorsScience, 1989
- Antigen Recognition by Class I-Restricted T LymphocytesAnnual Review of Immunology, 1989
- Structure of the human class I histocompatibility antigen, HLA-A2Nature, 1987
- Cytotoxic T cells recognize fragments of the influenza nucleoproteinCell, 1985
- Restriction of in vitro T cell-mediated cytotoxicity in lymphocytic choriomeningitis within a syngeneic or semiallogeneic systemNature, 1974