Hansen T, Balendiran G, Solheim J, Ostrov D, Nathenson S
Washington University School of Medicine, St Louis, MO 63110, USA.
Immunol Today. 2000 Feb;21(2):83-8. doi: 10.1016/s0167-5699(98)01426-1.
Comparisons of the structures of different mouse MHC class I molecules define how polymorphic residues determine the unique structural motif and atomic anchoring of their bound peptides. Here, Ted Hansen and colleagues speculate that quantitative differences in how class I molecules interact with peptide, beta2-microglobulin and molecular chaperones that facilitate peptide loading might determine their relative participation in different pathways of antigen presentation.
对不同小鼠MHC I类分子结构的比较,确定了多态性残基如何决定其结合肽的独特结构基序和原子锚定。在此,泰德·汉森及其同事推测,I类分子与肽、β2-微球蛋白以及促进肽负载的分子伴侣相互作用方式的定量差异,可能决定它们在不同抗原呈递途径中的相对参与程度。