Science Advances

This PDF file includes:

• Supplementary Text
• Fig. S1. Overall conformational changes of BRIL-DOP-KGCHM07 and BRIL-DOP-DPI-287 compared to other opioid receptor structures.
• Fig. S2. The importance of sodium-binding pocket mutations and DOP agonists for protein thermostability.
• Fig. S3. Effects of sodium-binding pocket mutations on DOP activation by DOP agonist DPI-287 and enhanced constitutive activity.
• Fig. S4. Differences between ligand recognition with different scaffolds by the DOP.
• Fig. S5. Water-mediated interactions during DOP activation.
• Fig. S6. The crystal lattice of the active-like BRIL-DOP structures is arranged in antiparallel dimers.
• Table S1. Pharmacological assessment of crystal structure construct mutants in WT (gray) or crystal structure construct background (blue) and ligand binding pocket mutants (green).
• Table S2. Assessment of conformational states with the “GAUGE” tool for the DOP and other opioid receptor structures.
• Table S3. Docking results for selected small-molecule and peptide DOP agonists.
• Table S4. Data collection and refinement statistics.

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