Substitution of aspartic acid at β57 with alanine alters MHC class II peptide binding activity but not protein stability: HLA-DQ (α1∗0201, β1∗0302) and (α1∗0201, β1∗0303)
- 31 December 1999
- journal article
- Published by Elsevier in Human Immunology
- Vol. 60 (12) , 1227-1236
- https://doi.org/10.1016/s0198-8859(99)00120-2
Abstract
No abstract availableKeywords
This publication has 45 references indexed in Scilit:
- Susceptibility to type I diabetes: HLA-DQ and DR revisitedImmunology Today, 1996
- Glutamic acid decarboxylase and other autoantigens in IDDMCurrent Opinion in Immunology, 1995
- Genetic Control of Autoimmune Diabetes in the Nod MouseAnnual Review of Immunology, 1995
- Self-peptides bound to the type I diabetes associated class II MHC molecules HLA-DQ1 and HLA-DQ8International Immunology, 1994
- Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptideNature, 1994
- Islet cell autoantigens in insulin-dependent diabetes.Journal of Clinical Investigation, 1993
- Three-dimensional structure of the human class II histocompatibility antigen HLA-DR1Nature, 1993
- Thermal Stability Comparison of Purified Empty and Peptide-Filled Forms of a Class I MHC MoleculeScience, 1992
- The human class II MHC protein HLA-DR1 assembles as empty αβ heterodimers in the absence of antigenic peptideCell, 1992
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970