Mediation by HLA-DM of dissociation of peptides from HLA-DR
Article Abstract:
Human leukocyte antigen (HLA)-DM may facilitate ligand exchange because binding assays using recombinant soluble heterodimers of HLA-DM obtained from Drosophila S2 cells show an increase in the amount of peptides bound to DR while also releasing DR-bound peptides at pH 5.0 or higher. DM probably increases the availability of DR to the peptides and has no effect on the affinity of peptides for DR. When the pH is 5.0 the dissociation of peptides bound to HLA-DR takes place probably by a change in the conformation of DR. DM ensures that the MHC class II molecules reach the cell surface bound to peptides whose dissociation rates are slow.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1995
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A metal complex that binds alpha-amino acids with high and predictable stereospecificity
Article Abstract:
It has been possible to establish a framework for stereospecific recognition of amino acids and, by implication, of structurally related molecules. It was established that a rationally designed metal complex created from a trivalent cobalt ion and a tetradentate ligand binds natural amino acids with high and predictable regio- and stereospecificity. It appears that the regiospecificity is controlled by electrostatic effects, while the stereospecificity is controlled by steric effects in a very predictable way.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1999
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HLA-E binds to natural killer cell receptors CD94/NKG2A, B and C
Article Abstract:
HLA-E is a protein which is a major histocompatibility complex (MHC), and its expression on the surface of cells is affected by peptides. Some other MHC molecules affct peptide binding, and so HLA-E expression. HLA alleles with leader peptides can upregulate the surface expression of HLA-E, and these alleles can provide resistance to lysis that is MK-cell-mediated. This means that HLA-E mediates their action. HLA-E is the main ligand for CD94/NKG2A, an inhibitory receptor for NK cells.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1999
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