HLA-DRα chain residues located on the outer loops are involved in nonpolymorphic and polymorphic antibody-binding epitopes

Author:

Fu Xin-Ting,Karr Robert W.

Publisher

Elsevier BV

Subject

General Medicine,Immunology,Immunology and Allergy

Reference54 articles.

1. 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 recognition;Barker;Hum Immunol,1991

2. Structural requirements for recognition of the HLA-Dw 14 class II epitope: a key HLA determinant associated with rheumatoid arthritis;Hiraiwa,1990

3. Transfer of polymorphic monoclonal antibody epitopes to the first and second domains of HLA-DR β-chain by site-directed mutagenesis;Maurer;J Immunol,1991

4. Identification of residues involved in polymorphic antibody binding epitopes on HLA-DR molecules;Fu;Hum Immunol,1992

5. Diverse locations of amino acids in HLA-DRβ chains involved in polymorphic antibody binding epitopes on DR(α,β1∗0101), DR(α,β1∗1101), and DR(α,β∗0202) molecules;Fu;Hum Immunol,1992

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