Residue 67 in the DR β1*0101 and DR β1*0103 chains strongly influences antigen presentation and DR-peptide molecular complex conformation

Author:

L'Faqihi F.-E.,Praud C.,Yassine-Diab B.,Enault G.,Lakhdar-Ghazal F.,Préval C.,Coppin H.

Publisher

Wiley

Subject

Genetics,Biochemistry,Immunology,General Medicine,Immunology and Allergy

Reference31 articles.

1. Effect of natural polymorphism at residue 86 of the HLA-DR|3 chain on peptide binding;Busch;J Immunol,1991

2. Single amino acid changes in DR and antigen define residues critical for peptide-MHC binding and T-cell recognition;Krieger;J Immunol,1991

3. Three-dimensional structure of the human class II histocompatibility antigen HLA-DR1;Brown;Nature,1993

4. Crystal structure of the human class II MHC protein HLA-DR1 complexed with an influenza virus peptide;Stern;Nature,1994

5. Identification of HLA-DR α chain residues critical for binding of the toxic shock syndrome toxin superantigen;Panina-Bordignon;J Exp Med,1992

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