Fig. 5: HDX MS identifies conformational changes upon G101V mutagenesis and the corrective influence of BAD SAHB 4.2 interaction. | Nature Communications

Fig. 5: HDX MS identifies conformational changes upon G101V mutagenesis and the corrective influence of BAD SAHB 4.2 interaction.

From: Structural insights into chemoresistance mutants of BCL-2 and their targeting by stapled BAD BH3 helices

Fig. 5

Deuterium difference plots showing the relative deuterium incorporation of BCL-2ΔC WT/BAD SAHB 4.2 minus BCL-2ΔC WT (a), BCL-2ΔC G101V/BAD SAHB 4.2 minus BCL-2ΔC G101V (b), BCL-2ΔC G101V minus BCL-2ΔC WT (c), and BCL-2ΔC G101V/BAD SAHB 4.2 minus BCL-2ΔC WT/BAD SAHB 4.2 (d), as measured at 10 s, 1 min, and 10 min of deuterium labeling. Regions of protection (green) above the 0.5-Da significance threshold (gray shading) at 1 min of deuterium labeling are mapped onto the structure of BAD SAHB 4.2/BCL-2ΔLΔC WT or G101V (PDB 9O14, 9O15). The protein, stapled peptide, and mutant residue are colored gray, maroon, and red, respectively. Peptides containing the point mutation cannot be compared to WT and are thus represented by bracketed gaps in the plots (c, d). HDX MS experiments were performed twice using independent preparations of BCL-2 proteins and reagents. ND no data. Source data are provided as Supplementary Data 1.

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