Abstract
This report describes a detailed mutational analysis of a major histocompatibility complex class II moleculethe a 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.
Original language | English |
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Pages (from-to) | 4215-4223 |
Number of pages | 9 |
Journal | EMBO Journal |
Volume | 9 |
Issue number | 13 |
State | Published - 1990 |
Keywords
- Antigen presentation
- Major histocompatibility complex
- Site-specific mutagenesis
- T cell recognition