Alteration within a discrete region of the H-2Ld alpha 1 helix upon association with human beta 2 microglobulin.
The utilization of the beta 2-microglobulin (B2m) exchange assay allowed for the association of H-2Ld with human B2m. Upon association with H-2Ld, human B2m induces structural alterations in H-2Ld that appear dependent upon xenogeneic B2m amino acid sequence variability. In this regard, xenogeneic B2m exchange is used as a tool to induce structural alterations in class I as a means of analysing the structural-functional relationship of B2m/class I association. Incorporating H-2Ld site-directed mutants into the experimental approach provided strong evidence that B2m makes indirect contact with discrete class I specific amino acid positions located in the helical region of the alpha 1 domain.
Smith
M J
MJ
Department of Biological Sciences, California State University, Hayward 94542.
Basora
T
T
Kieran
J E
JE
Nieto
M C
MC
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D002460:Cell Line; D006183:H-2 Antigens / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D064532:Histocompatibility Antigen H-2D; D006801:Humans; D051379:Mice; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D011485:Protein Binding; D017433:Protein Structure, Secondary; D001613:beta 2-Microglobulin / Q000378:metabolism*
D006183:H-2 Antigens; D064532:Histocompatibility Antigen H-2D; D001613:beta 2-Microglobulin