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. 2026 Aug 4;136(19):e201406. doi: 10.1172/JCI201406

Figure 2. S100A11 can bind to cholesterol.

Figure 2

(A) The recombinant human S100A11 protein dimer structure (left, Protein Databank [PDB] ID: 2LUC) and its corresponding topological model (right). Light purple and green helices (left) and boxes (right) represent the 5 helical regions of the 2 monomers, respectively. Dark blue and red arrows indicate the 2 β-strands of each monomer. The amino acids shown in red indicate potential cholesterol-binding sites on S100A11. (B) Molecular docking results for S100A11 with cholesterol. The predicted pocket positions of cholesterol interaction with S100A11 amino acid residues are shown. (C) Results for potential sites of S100A11 binding to cholesterol, the corresponding binding energies, and the hydrogen bonding distances. (D) Assay of S100A11 protein binding to the membrane lipid strip. (E) Colocalization of S100A11 with the FC stained by filipin and the ER marker calnexin in Huh7 cells. Scale bars: 10 μm. (F and G) Western blot analysis of S100A11 protein in Huh7 (F) and Hepa1–6 (G) cells treated with cholesterol (Chol), U18666A, or their combination (n = 3). Graphs show the quantification. (H) Schematic diagram of GFP-tagged S100A11 truncations. (I) Western blot analysis of S100A11 point-mutant protein in Huh7 cells treated with cholesterol. (J) Fluorescent expression of GFP-tagged S100A11 point mutations in Huh7 cells treated with cholesterol. Scale bars: 10 μm. (K) Cholesterol binding curves for WT and point mutation S100A11 proteins measured by MST. GAPDH or tubulin was used as an internal control for Western blot analysis. Data are presented as the mean ± SEM. Data were compared using 1-way ANOVA with Dunnett’s test. ***P < 0.001.