The three-dimensional structure of H-2Db at 2.4 Å resolution: Implications for antigen-determinant selection
- 14 January 1994
- Vol. 76 (1) , 39-50
- https://doi.org/10.1016/0092-8674(94)90171-6
Abstract
No abstract availableKeywords
This publication has 33 references indexed in Scilit:
- The three-dimensional structure of HLA-B27 at 2.1 Å resolution suggests a general mechanism for tight peptide binding to MHCCell, 1992
- Crystal Structures of Two Viral Peptides in Complex with Murine MHC Class I H-2K bScience, 1992
- Characterization of Peptides Bound to the Class I MHC Molecule HLA-A2.1 by Mass SpectrometryScience, 1992
- The structure of HLA-B27 reveals nonamer self-peptides bound in an extended conformationNature, 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
- Isolation of an endogenously processed immunodominant viral peptide from the class I H–2Kb moleculeNature, 1990
- STRUCTURE, FUNCTION, AND DIVERSITY OF CLASS I MAJOR HISTOCOMPATIBILITY COMPLEX MOLECULESAnnual Review of Biochemistry, 1990
- An efficient general-purpose least-squares refinement program for macromolecular structuresActa Crystallographica Section A Foundations of Crystallography, 1987
- The epitopes of influenza nucleoprotein recognized by cytotoxic T lymphocytes can be defined with short synthetic peptidesCell, 1986