Anchor residue motifs of HLA class-I-binding peptides analyzed by the direct binding of synthetic peptides to HLA class I α chains
✍ Scribed by Fruci, Doriana; Rovero, Paolo; Falasca, Giuliana; Chersi, Alberto; Sorrentino, Rosa; Butler, Richard; Tanigaki, Nobuyuki; Tosi, Roberto
- Book ID
- 123358559
- Publisher
- Elsevier Science
- Year
- 1993
- Tongue
- English
- Weight
- 451 KB
- Volume
- 38
- Category
- Article
- ISSN
- 0198-8859
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Eight nonamer peptides that comply with the major anchor residue motifs (the combination of amino acid residues at positions 2 and 9), R - K and R - R, of HLA-B27 (B\*2705)-binding peptides were synthesized and tested for their direct binding to HLA class I alpha chains by the HLA class I alpha chai
## Abstract A direct binding assay has been used to investigate the effect of the secondary anchor residues on peptide binding to class I proteins of the major histocompatibility complex. Based on predictions from a previous chemometric approach, synthetic peptide analogues containing unnatural ami