Delineation of antigen contact residues on an MHC class II molecule.
J Peccoud, P Dellabona, P Allen, C Benoist… - The EMBO …, 1990 - embopress.org
J Peccoud, P Dellabona, P Allen, C Benoist, D Mathis
The EMBO Journal, 1990•embopress.orgThis 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 …
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 …
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.
embopress.org