ArticleImmunogenetics2004
A single amino-acid polymorphism in pocket A of HLA-A*6602 alters the auxiliary anchors compared with HLA-A*6601 ligands.
Article in Immunogenetics, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 24 citations in OpenAlex.
- Article
- Understanding the obstacle of incompatibility at residue 156 within HLA-B*35 subtypes.Immunogenetics · 2016Article
- The diversity of the HLA-E-restricted peptide repertoire explains the immunological impact of the Arg107Gly mismatch.Immunogenetics · 2016Article
- HLA-E: Presentation of a Broader Peptide Repertoire Impacts the Cellular Immune Response-Implications on HSCT Outcome.Stem cells international · 2015Article
- Residue 81 confers a restricted C-terminal peptide binding motif in HLA-B*44:09.Immunogenetics · 2012Article
- Position 45 influences the peptide binding motif of HLA-B*44:08.Immunogenetics · 2012Article
- Modulatory role of calreticulin as chaperokine for dendritic cell-based immunotherapy.Clinical and experimental immunology · 2011Article
- Large-scale characterization of peptide-MHC binding landscapes with structural simulations.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- The impact of human leukocyte antigen (HLA) micropolymorphism on ligand specificity within the HLA-B*41 allotypic family.Haematologica · 2011Article
- The nature of peptides presented by an HLA class I low expression allele.Haematologica · 2010Article
- Amino acid 95 causes strong alteration of peptide position Pomega in HLA-B*41 variants.Immunogenetics · 2007Article
- A modular concept of HLA for comprehensive peptide binding prediction.Immunogenetics · 2007Article
- Peptide-binding motif of HLA-A*6603.Immunogenetics · 2005Article
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6 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
In this study we have sequenced peptides eluted from a truncated recombinant HLA-A*6602 molecule, and compared their features with data reported for peptides presented in the A*6601 molecule. A striking change in the amino-acid binding preferences was observed at peptide position P1, which interacts with pocket A of the HLA peptide-binding region. For A*6601, aspartic acid and glutamic acid, both of which possess polar acidic side-chains, have been described as auxiliary anchors. This is in marked contrast to A*6602, where we observed serine, which has a neutral polar side-chain, as auxiliary anchor at P1. Accordingly, this shift in the physico-chemical properties of the auxiliary anchor may be best explained by the HLA amino-acid polymorphism at position 163, where arginine (hydrophilic, alkaline) in A*6601 has been replaced by glutamic acid in A*6602. This amino-acid exchange results in a shift towards higher acidity in pocket A, apparently resulting in the loss of preference for acidic auxiliary anchors, and leading to the preference for the neutral amino acid serine. The change of the auxiliary anchor residue at P1 is likely to alter the spectrum of peptides presented by A*6602 compared with A*6601, which may result in allogenicity in the case of a mismatch in allogeneic stem cell transplantation.
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