Identification of HLA-DR9 (DRB1∗ 0901)-binding peptide motifs using a phage fUSE5 random peptide library
S Fujisao, S Matsushita, T Nishi, Y Nishimura - Human immunology, 1996 - Elsevier
We identified HLA-DRB1∗ 0901-binding peptides by affinity-based selection of a phage
random peptide library using the biotinylated DR9 complex. Analogue peptides with single
amino acid residue substitutions of a DR9 binder revealed that two major anchors (WxxS,
where x is any amino acid) play an essential role in binding to DR9. Determination of the
binding affinity of synthetic wild-type-based analogue peptides showed that substituting W to
F or L, and S to A, V, or F allow high affinity binding with DR9. Collectively, DR9-binding …
random peptide library using the biotinylated DR9 complex. Analogue peptides with single
amino acid residue substitutions of a DR9 binder revealed that two major anchors (WxxS,
where x is any amino acid) play an essential role in binding to DR9. Determination of the
binding affinity of synthetic wild-type-based analogue peptides showed that substituting W to
F or L, and S to A, V, or F allow high affinity binding with DR9. Collectively, DR9-binding …
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