
doi: 10.1038/329506a0
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.
Models, Molecular, Binding Sites, Protein Conformation, Membrane Proteins, HLA Antigens, HLA-A2 Antigen, Computer Graphics, Animals, Humans, Antigens, beta 2-Microglobulin, Glycoproteins, Protein Binding
Models, Molecular, Binding Sites, Protein Conformation, Membrane Proteins, HLA Antigens, HLA-A2 Antigen, Computer Graphics, Animals, Humans, Antigens, beta 2-Microglobulin, Glycoproteins, Protein Binding
| selected citations These citations are derived from selected sources. This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | 4K | |
| popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network. | Top 0.1% | |
| influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically). | Top 0.01% | |
| impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network. | Top 0.01% |
