Qa-2 molecules are peptide receptors of higher stringency than ordinary class I molecules
CLASS I molecules of the major histocompatibility complex (MHC) transport peptides to the cell surface for surveillance by T cells 1 . Ligand specificity is stringent and differs from allele to allele 2–4 . Here we report analysis of natural ligands of 'unconventional' glycophosphatidyl-an...
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Veröffentlicht in: | Nature (London) 1993-02, Vol.361 (6413), p.642-644 |
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Zusammenfassung: | CLASS I molecules of the major histocompatibility complex (MHC) transport peptides to the cell surface for surveillance by T cells
1
. Ligand specificity is stringent and differs from allele to allele
2–4
. Here we report analysis of natural ligands of 'unconventional' glycophosphatidyl-anchored mouse class I molecules, Qa-2. The function of these molecules is unclear
5–6
; they can serve as recognition structures for 'unrestricted' cytotoxic T cells but have not been found to present peptides to T cells, although the DNA sequence suggests a similar peptide binding groove to that of 'conventional' class I molecules
7
, and other unconventional class I molecules can present antigens in a few cases
8–10
. Pool sequencing of natural Qa-2 ligands shows that Qa-2 molecules are indeed peptide receptors, having ligand specificity similar to that of conventional class I molecules, that is, a predominant length of nine amino acids, anchor positions, and hydrophobic termination of peptides. But ligand specificity is much more stringent than with other class I molecules: of the nine positions, two are anchors and four have rather limited occupancy. |
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ISSN: | 0028-0836 1476-4687 |
DOI: | 10.1038/361642a0 |