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| Item Type: | Article |
|---|---|
| Title: | Qa-2 molecules are peptide receptors of higher stringency than ordinary class I molecules |
| Creators Name: | Roetzschke, O., Falk, K., Stevanovic, S., Grahovac, B., Soloski, M.J., Jung, G. and Rammensee, H.G. |
| Abstract: | 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. |
| Keywords: | Amino Acid Sequence, Binding Sites, Histocompatibility Antigens Class I, Inbred C57BL Mice, Molecular Sequence Data, Peptides, Animals, Mice |
| Source: | Nature |
| ISSN: | 0028-0836 |
| Publisher: | Nature Publishing Group |
| Volume: | 361 |
| Number: | 6413 |
| Page Range: | 642-644 |
| Date: | 18 February 1993 |
| Official Publication: | https://doi.org/10.1038/361642a0 |
| PubMed: | View item in PubMed |
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