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Molecules encoded by the major histocompatibility complex (MHC) are polymorphic integral membrane proteins adapted to the presentation of peptide fragments of foreign antigens to antigen-specific T-cells. The diversity of infectious agents to which an immune response must be mounted poses a unique problem for receptor-ligand interactions; how can proteins whose polymorphism is necessarily limited bind an array of peptides almost infinite in its complexity? Both MHC class I and class II determinants have achieved this goal by harnessing a limited number of peptide side chains to anchor the epitope in place while exploiting conserved features of peptide structure, independent of their primary sequence. While class I molecules interact predominantly with the N- and C-termini of peptides, class II determinants form an extensive hydrogen bonding network along the length of the peptide backbone. Such a strategy ensures high-affinity binding, while selectively exposing the unique features of each ligand for recognition by the T-cell receptor.

Original publication

DOI

10.1002/(SICI)1099-1387(199805)4:3%3C182::AID-PSC144%3E3.0.CO;2-S

Type

Journal article

Journal

J Pept Sci

Publication Date

05/1998

Volume

4

Pages

182 - 194

Keywords

Animals, Epitopes, Histocompatibility Antigens Class I, Histocompatibility Antigens Class II, Humans, Major Histocompatibility Complex, Peptides, Receptors, Antigen, T-Cell