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Extra resources for Antigen Delivery Systems: Immunological and Technological Issues (Drug Targeting and Delivery)
Mol. , 33, 387–397. K.
This mode of antigen recognition consequently depends on the sequence of the determinants rather than the tridimensional structure of the antigens. Thus, determinants which are buried in a folded polypeptide can nevertheless be released for recognition by T cells. While antibodies are intended to bind antigens encountered in the extracellular milieu, T lymphocytes have the capacity to detect antigens taken up by other cells, as well as antigens residing in cells. That antigen recognition relies on different mechanisms decreases the likelihood that a pathogen could succeed to deceive the immune system.
The membrane-distal domains, the α1 and β1, which contain most of the polymorphic residues between alleles, constitute the peptide binding site. This structure is formed by a floor of 8 βplated sheets on which lay two α-helices. The antigen fragments are bound in the groove between the helices (Madden, 1995). , 1993). , (1988) on the basis of a similar arrangement of clusters of polymorphic and conserved residues between class I and class II polypeptides, the structures of class I and class II MHC heterodimers are closely related.