A tricyclic ring system replaces the variable regions of peptides presented by three alleles of human MHC class I molecules
- 30 June 1995
- journal article
- Published by Elsevier in Chemistry & Biology
- Vol. 2 (6) , 401-407
- https://doi.org/10.1016/1074-5521(95)90221-x
Abstract
No abstract availableKeywords
This publication has 21 references indexed in Scilit:
- Importance of Peptide Amino and Carboxyl Termini to the Stability of MHC Class I MoleculesScience, 1994
- Effects of Peptide Length and Composition on Binding to an Empty Class I MHC HeterodimerBiochemistry, 1994
- Antigenic peptide binding by class I and class II histocompatibility proteinsStructure, 1994
- The Biochemistry and Cell Biology of Antigen Processing and PresentationAnnual Review of Immunology, 1993
- Thermal Stability Comparison of Purified Empty and Peptide-Filled Forms of a Class I MHC MoleculeScience, 1992
- The three-dimensional structure of HLA-B27 at 2.1 Å resolution suggests a general mechanism for tight peptide binding to MHCCell, 1992
- Characterization of Peptides Bound to the Class I MHC Molecule HLA-A2.1 by Mass SpectrometryScience, 1992
- Identification of self peptides bound to purified HLA-B27Nature, 1991
- Allele-specific motifs revealed by sequencing of self-peptides eluted from MHC moleculesNature, 1991
- Refined structure of the human histocompatibility antigen HLA-A2 at 2.6 Å resolutionJournal of Molecular Biology, 1991