HLA class I binding motifs derived from random peptide libraries differ at the COOH terminus from those of eluted peptides.

Journal article

Recombinant HLA-A2, HLA-B8, or HLA-B53 heavy chain produced in Escherichia coli was combined with recombinant beta2-microglobulin (beta2m) and a pool of randomly synthesised nonamer peptides. This mixture was allowed to refold to form stable major histocompatability complex (MHC) class I complexes, which were then purified by gel filtration chromatography. The peptides bound to the MHC class I molecules were subsequently eluted and sequenced as a pool. Peptide binding motifs for these three M...

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Authors: Davenport, M; Smith, K; Barouch, D; Reid, S; Bodnar, WM

• Publication status: Published
• Journal: Journal of experimental medicine
• Volume: 185
• Issue: 2
• Pages: 367-371
• Publication date: 1997-01-01
• DOI: 10.1084/jem.185.2.367
• EISSN: 1540-9538
• ISSN: 0022-1007
• Language: English
• Keywords: Humans; Amino Acid Sequence; Peptide Library; Cloning, Molecular; Escherichia coli; Chromatography, Gel; Molecular Sequence Data; Binding Sites; HLA Antigens