Different regions of the N-terminal domains of HLA-DR1 influence recognition of individual peptide-DR1 complexes
- 31 August 1994
- journal article
- Published by Elsevier in Human Immunology
- Vol. 40 (4) , 312-322
- https://doi.org/10.1016/0198-8859(94)90031-0
Abstract
No abstract availableKeywords
This publication has 43 references indexed in Scilit:
- T cell receptor interaction with peptide/major histocompatibility complex (MHC) and superantigen/MHC ligands is dominated by antigen.The Journal of Experimental Medicine, 1993
- Three-dimensional structure of the human class II histocompatibility antigen HLA-DR1Nature, 1993
- A molecular model of MHC class-I-restricted antigen processingImmunology Today, 1992
- Predominant naturally processed peptides bound to HLA-DR1 are derived from MHC-related molecules and are heterogeneous in sizeNature, 1992
- Effects of localized HLA class II β chain polymorphism on binding of antigenic peptide and stimulation of T cellsHuman Immunology, 1992
- Contribution of T-cell receptor-contacting and peptide-binding residues of the class II molecule HLA-DR4 Dw10 to serologic and antigen-specific T-cell recognitionHuman Immunology, 1991
- Refined structure of the human histocompatibility antigen HLA-A2 at 2.6 Å resolutionJournal of Molecular Biology, 1991
- The molecular basis of alloreactivityImmunology Today, 1990
- Implications of a Fab-like structure for the T-cell receptorImmunology Today, 1989
- T-cell antigen receptor genes and T-cell recognitionNature, 1988