Fig. 2: Selection and analysis of a yeast-displayed HLA-DR401 randomized peptide library. | Nature Communications

Fig. 2: Selection and analysis of a yeast-displayed HLA-DR401 randomized peptide library.

From: Repertoire-scale determination of class II MHC peptide binding via yeast display improves antigen prediction

Fig. 2

a Schematic of sequential rounds of library selection to eliminate non-binding peptides and enrich binders. b Unweighted heat maps of positional percent frequency and log2-fold enrichment of each amino acid in round 5 of selection (n = 81,422 unique peptides). c Structure of HA306-318 peptide in the HLA-DR401 peptide-binding groove (PDB 1J8H), with primary peptide MHC anchor positions denoted. d Kullback–Leibler relative entropy motifs of the core nine amino acids of HLA-DR401-binding peptides, as determined empirically from our yeast-display library, or by clustering of binders curated on the SYFPEITHI database.

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