Abstract
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.
Publication types
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Research Support, U.S. Gov't, P.H.S.
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Review
MeSH terms
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Animals
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Antigen Presentation* / immunology
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Antiporters / metabolism
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Calcium-Binding Proteins / metabolism
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Calreticulin
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Histocompatibility Antigens Class I / chemistry*
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Histocompatibility Antigens Class I / metabolism
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Histocompatibility Antigens Class I / physiology*
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Immunoglobulins / metabolism
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Membrane Transport Proteins
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Mice
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Molecular Conformation
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Peptides / metabolism
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Ribonucleoproteins / metabolism
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beta 2-Microglobulin / metabolism
Substances
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Antiporters
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Calcium-Binding Proteins
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Calreticulin
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Histocompatibility Antigens Class I
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Immunoglobulins
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Membrane Transport Proteins
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Peptides
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Ribonucleoproteins
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beta 2-Microglobulin
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tapasin