Loftus D J, Kubo R T, Sakaguchi K, Celis E, Sette A, Appella E
Laboratory of Cell Biology, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892, USA.
Adv Exp Med Biol. 1995;383:201-10. doi: 10.1007/978-1-4615-1891-4_21.
The structural features which underlie peptide binding to MHC molecules permit the binding of a diverse array of peptides. Polymorphic residues of class I, and to a lesser extent, class II molecules, determine the peptide selectivities associated with various allomorphs. The motifs which are described here and elsewhere in the literature mainly reflect peptide features which contribute to high affinity binding. While high affinity MHC binding is not an absolute prerequisite for the immunologic relevance of a peptide, motifs provide general guidelines for eliciting and characterizing cellular responses to epitopes presented by a given MHC allomorph or group of related allomorphs. The utility of motifs is underscored by emerging developments in the clinical application of peptides to elicit specific and effective cellular responses.
肽与MHC分子结合的结构特征使得多种不同的肽能够与之结合。I类分子的多态性残基,以及程度稍轻的II类分子的多态性残基,决定了与各种同种异型相关的肽选择性。本文及文献其他地方所描述的基序主要反映了有助于高亲和力结合的肽特征。虽然高亲和力的MHC结合对于肽的免疫相关性并非绝对必要条件,但基序为引发和表征针对给定MHC同种异型或一组相关同种异型所呈递表位的细胞反应提供了一般指导原则。肽在临床应用中引发特异性和有效细胞反应的新进展突出了基序的实用性。