Structure of the human class I histocompatibility antigen, HLA-A2.
The class I histocompatibility antigen from human cell membranes has two structural motifs: the membrane-proximal end of the glycoprotein contains two domains with immunoglobulin-folds that are paired in a novel manner, and the region distal from the membrane is a platform of eight antiparallel beta-strands topped by alpha-helices. A large groove between the alpha-helices provides a binding site for processed foreign antigens. An unknown 'antigen' is found in this site in crystals of purified HLA-A2.
Bjorkman
P J
PJ
Department of Biochemistry and Molecular Biology, Harvard University, Cambridge, Massachusetts 02138.
Saper
M A
MA
Samraoui
B
B
Bennett
W S
WS
Strominger
J L
JL
Wiley
D C
DC
D000941:Antigens / Q000378:metabolism; D001665:Binding Sites; D003196:Computer Graphics; D006023:Glycoproteins / Q000378:metabolism; D006680:HLA Antigens / Q000378:metabolism; D015789:HLA-A2 Antigen; D006801:Humans; D008565:Membrane Proteins / Q000378:metabolism; D008958:Models, Molecular; D011485:Protein Binding; D011487:Protein Conformation; D001613:beta 2-Microglobulin / Q000378:metabolism
D000941:Antigens; D006023:Glycoproteins; D006680:HLA Antigens; D015789:HLA-A2 Antigen; D008565:Membrane Proteins; D001613:beta 2-Microglobulin