This PDF file includes:

• Supplementary Materials and Methods
• fig. S1. Cellular characterization of LSD1 reversible inhibitors.
• fig. S2. Comparison of polymyxin B and polymyxin E conformations from multiple data sets.
• fig. S3. Characterization of the binding of E11 to LSD1-CoREST in solution by isothermal titration calorimetry.
• fig. S4. Noncovalent quinazoline-derived compound MC3767 binds the LSD1 active site in a multiple stacking assembly as E11.
• fig. S5. Workflow of the PDB search for multicopy stacking small-molecule inhibitors.
• fig. S6. Comparison of histone methyltransferase G9a-like protein (GLP) and histone demethylase LSD1 in complex with compound E11.
• fig. S7. LSD1 druggable space is expanded by the binding of noncovalent compounds.
• table S1. Diffraction, data collection, and refinement statistics.
• table S2. Diffraction, data collection, and refinement statistics for all data sets of polymyxins B and E.
• table S3. List of protein inhibitor structures displaying multiple stacking conformation identified from PDB search.
• table S4. List of published LSD1 PDB structures in complex with ligands.
• References (37–55)

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