Fig. 3: Phosphorylated OPTN158–191 causes changes in solvent accessibility of charged residues of LC3B at the interaction interface.
From: Decoding phospho-regulation and flanking regions in autophagy-associated short linear motifs
A–C Relative solvent-accessible surface area (SASA) of side chain atoms for K51 (A), K49 (B), and D48 (C) is shown across three replicates (n = 100,000 frames each) per system, along with comparative simulations based on the NMR structure of the LC3B–OPTN complex (n = 100,000 frames). The main systems (LC3B1−120–OPTN158–191, LC3B1–120–p1OPTN158–191, and LC3B1–120–p5OPTN158–191) are derived from AlphaFold models, while the comparative simulations were initialized from the first conformer of the NMR structure 2LUE (residues 169–185 of OPTN and 1–120 of LC3B), with matching phosphorylation patterns. Each box represents the interquartile range (IQR, 25th to 75th percentile), with the horizontal line inside the box indicating the median. Whiskers extend to data points within 1.5×IQR from the lower and upper quartiles. Outliers are not shown. The AlphaFold-based models include a longer OPTN fragment (residues 158–191), and during simulations, the additional flanking regions can transiently shield LC3B residues such as D48 and K51, potentially reducing their solvent accessibility relative to the shorter experimental construct.
