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Cell. 1993 Jul 16;74(1):197-203.

Promiscuous and allele-specific anchors in HLA-DR-binding peptides.

Author information

1
Roche Milano Ricerche, Italy.

Abstract

The major histocompatibility complex (MHC) class II molecules are highly polymorphic membrane glycoproteins that bind peptide fragments of proteins and display them for recognition by CD4+ T cells. To understand the effect of human MHC class II polymorphism on peptide-MHC interaction, we have isolated M13 phage from a large M13 peptide display library by selection with DRB1*0401 and DRB1*1101 molecules, as recently described for DRB1*0101. Sequence analysis of the peptide-encoding region of DR-bound phage led to the identification of position-specific anchor residues, defining motifs for peptide binding to DR molecules. The three DR motifs share two anchor residues at relative positions 1 and 4, while allele-specific anchor residues have been identified at position 6. These results provide a biophysical basis for both the promiscuity and the specificity of peptide recognition by DR molecules.

PMID:
8334703
DOI:
10.1016/0092-8674(93)90306-b
[Indexed for MEDLINE]

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