The structure of HLA-B27 reveals nonamer self-peptides bound in an extended conformation
- 1 September 1991
- journal article
- research article
- Published by Springer Nature in Nature
- Vol. 353 (6342) , 321-325
- https://doi.org/10.1038/353321a0
Abstract
X-ray crystallography reveals electron density in the antigen-binding site of HLA-B27 that is an interpretable image of nonameric peptides in a largely extended conformation. Clear density exists for the main chain and several side chains and is consistent with the sequence of 11 nonameric self-peptides eluted from HLA-B27 (see accompanying article1). Pockets in the antigen-binding cleft bind four side chains and the amino and carboxyl termini of the peptide.Keywords
This publication has 38 references indexed in Scilit:
- Identification of self peptides bound to purified HLA-B27Nature, 1991
- Allele-specific motifs revealed by sequencing of self-peptides eluted from MHC moleculesNature, 1991
- Peptide binding to empty HLA-B27 molecules of viable human cellsNature, 1991
- Refined structure of the human histocompatibility antigen HLA-A2 at 2.6 Å resolutionJournal of Molecular Biology, 1991
- Isolation and analysis of naturally processed viral peptides as recognized by cytotoxic T cellsNature, 1990
- Isolation of an endogenously processed immunodominant viral peptide from the class I H–2Kb moleculeNature, 1990
- Structural homologies between two HLA B27-restricted peptides suggest residues important for interaction with HLA B27International Immunology, 1990
- Antigen Recognition by Class I-Restricted T LymphocytesAnnual Review of Immunology, 1989
- Methods and programs for direct-space exploitation of geometric redundanciesActa Crystallographica Section A, 1976
- A method of positioning a known molecule in an unknown crystal structureActa Crystallographica, 1967