Abstract
This report describes a detailed mutational analysis of a major histocompatibility complex class II molecule--the alpha chain of the Ak complex. Each residue from 50-79 was replaced by an alanine, and the effects on recognition of Ak by panels of antibodies and T cells determined. The results provide the strongest existing experimental evidence that the antigen binding site on a class II molecule can be modelled on the crystal structure of a class I molecule. The data have also permitted the delineation of residues that actually contact antigenic peptides.
Publication types
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Alanine / genetics
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Amino Acid Sequence
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Animals
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Antibodies, Monoclonal / immunology
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Binding, Competitive
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Histocompatibility Antigens Class II / chemistry*
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Histocompatibility Antigens Class II / immunology
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Hybridomas / immunology
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Mice
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Mice, Inbred Strains
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Models, Molecular
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Molecular Sequence Data
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Muramidase / genetics*
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Muramidase / immunology
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Mutagenesis, Site-Directed
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Peptide Fragments / genetics*
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Peptide Fragments / immunology
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Protein Conformation
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Reproducibility of Results
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Ribonucleases / genetics*
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Ribonucleases / immunology
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T-Lymphocytes / immunology
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X-Ray Diffraction
Substances
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Antibodies, Monoclonal
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Histocompatibility Antigens Class II
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Peptide Fragments
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bovine ribonuclease peptide (41-61)
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hen egg lysozyme peptide (46-61)
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Ribonucleases
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Muramidase
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Alanine