Fig. 5: ASK1–MAX2–HTL7–SMAX1 complex dynamics and receptor specificity.
A Each black bar represents a peptide of HTL7 identified in hydrogen-deuterium exchange (HDX) coupled with mass spectrometry (HDX-MS) experiments. The difference in HDX of pairwise comparisons between HTL7-containing samples is displayed on its amino acid sequences. Different tones of red and blue indicate HTL7 residues that incorporate more or less deuterium, respectively, in the first state of the pairwise comparison. A numbered list of tested conditions is provided, with each component name coloured based on the reference view in panel (D). B Deuterium-enriched peptides mapped on the open (PDB 5Z8P) and closed structure of HTL7 from this study (PDB 9KKX). C Protected regions of HTL7 + GR24 and MAX2 in complex with SMAX1 mapped on the structure (PDB 9KLV). The black coloured regions had no peptide coverage. D Reference view (left) of ASK1–MAX2–HTL7–SMAX1 (EMD-62417) with a white box outlining the focal area. Interface of MAX2–HTL7–SMAX1D2 (middle, 9KLD) and OsD3–AtD14–SMXL7D2 (right, PDB 5HZG). The SMAX1D2/SMXL7D2 (dark pink/light pink) RGKT motif and interface residues with HTL7/AtD14 are shown as sticks and coloured grey. HTL7/AtD14 are shown as a surface and coloured by electrostatic potential from red (negatively charged) to blue (positively charged). MAX2/OsD3 are coloured green.
