Structural features of MHC class I molecules that might facilitate alternative pathways of presentation.
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.
Hansen
T
T
Washington University School of Medicine, St Louis, MO 63110, USA. hansen@genetics.wustl.edu
Balendiran
G
G
Solheim
J
J
Ostrov
D
D
Nathenson
S
S
D000818:Animals; D017951:Antigen Presentation / Q000276:immunology; D017920:Antiporters / Q000378:metabolism; D002135:Calcium-Binding Proteins / Q000378:metabolism; D037282:Calreticulin; D015395:Histocompatibility Antigens Class I / Q000737:chemistry* / Q000378:metabolism / Q000502:physiology*; D007136:Immunoglobulins / Q000378:metabolism; D026901:Membrane Transport Proteins; D051379:Mice; D008968:Molecular Conformation; D010455:Peptides / Q000378:metabolism; D012261:Ribonucleoproteins / Q000378:metabolism; D001613:beta 2-Microglobulin / Q000378:metabolism
D017920:Antiporters; D002135:Calcium-Binding Proteins; D037282:Calreticulin; D015395:Histocompatibility Antigens Class I; D007136:Immunoglobulins; D026901:Membrane Transport Proteins; D010455:Peptides; D012261:Ribonucleoproteins; D001613:beta 2-Microglobulin; C107762:tapasin