Structural aspects of allorecognition.
The phenomenon of T-cell allorecognition of foreign major histocompatibility molecules has been one of the more enigmatic aspects of T-cell immunology. The molecular basis for allorecognition is unfolding as a result of the application of major histocompatibility complex structure/function analyses in the light of current insights into the three-dimensional structure of major histocompatibility complex products.
Lechler
R
R
Royal Postgraduate Medical School, London, UK.
Lombardi
G
G
D000818:Animals; D015395:Histocompatibility Antigens Class I / Q000276:immunology; D000949:Histocompatibility Antigens Class II / Q000276:immunology; D006801:Humans; D007111:Immunity, Cellular; D007519:Isoantigens / Q000276:immunology; D008285:Major Histocompatibility Complex; D010446:Peptide Fragments / Q000276:immunology; D011110:Polymorphism, Genetic; D011487:Protein Conformation; D011948:Receptors, Antigen, T-Cell / Q000276:immunology; D013329:Structure-Activity Relationship; D013601:T-Lymphocytes / Q000276:immunology*
D015395:Histocompatibility Antigens Class I; D000949:Histocompatibility Antigens Class II; D007519:Isoantigens; D010446:Peptide Fragments; D011948:Receptors, Antigen, T-Cell