Qa-2 molecules are peptide receptors of higher stringency than ordinary class I molecules (CROSBI ID 208934)
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Podaci o odgovornosti
Rötzschke, Olaf ; Falk, Kirsten ; Stevanović, Stefan ; Grahovac, Blaženka ; . Soloski, Mark J ; Jung, Gunther ; Rammensee, Hans-Georg
engleski
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. Ligand specificity is stringent and differs from allele to allele. Here we report analysis of natural ligands of 'unconventional' glycophosphatidyl- anchored mouse class I molecules, Qa-2. The function of these molecules is unclear ; 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, and other unconventional class I molecules can present antigens in a few cases. 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.
Qa-2 molecules
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