Fig. 5: Peptide conformational change influences specificity.
From: Hydrophobic interactions dominate the recognition of a KRAS G12V neoantigen
a Differential scanning fluorimetry analysis of KRASWT-HLA-A*03:01 (black) and KRASG12V-HLA-A*03:01 (blue). The negative derivative of relative fluorescence unit vs temperature is shown for each. The melting temperatures are labeled and correspond to the minimum peak of each first derivative. b Structural alignment of the KRASWT-HLA-A*03:01 (peptide, black sticks; HLA, yellow ribbons) and V2-Fab/KRASG12V-HLA-A*03:01 (peptide, blue sticks; HLA, gray ribbons) structures, highlighting the peptide binding groove. c The same structural alignment as in (b), with further zoom-in highlighting the conformational change within the KRASG12V peptide upon V2-Fab binding.
