Fig. 3: The presence of phosphoserine at P4 causes unique local conformational changes at the peptide-MHC binding site. | Nature Communications

Fig. 3: The presence of phosphoserine at P4 causes unique local conformational changes at the peptide-MHC binding site.

From: Molecular mechanism of phosphopeptide neoantigen immunogenicity

Fig. 3: The presence of phosphoserine at P4 causes unique local conformational changes at the peptide-MHC binding site.The alternative text for this image may have been generated using AI.

The amino acid residues are drawn as sticks. The Ile66 alternate conformations are marked by arrows. H-bonds (distance cutoff <3.5 Å) are the dotted lines between peptide and Arg62 or Gln155 residues, respectively. a Cartoon representation of the MLL747–755/HLA-B*0702 structure, carbons are yellow. b Cartoon representation of the OSE-MLL747–755/HLA-B*0702 structure, peptide carbons are gray. c Cartoon representation of the E7P-MLL747–755/HLA-B*0702 structure, peptide carbons are gray. d Superimposition of the E7P-MLL747–755/HLA-B*0702 (carbon atoms are yellow) and pMLL747–755/HLA-B*0702 crystal structures. H-bonds are shown between E7P-MLL747–755 and Arg62 or Gln155.

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