Science Advances
Supplementary Materials
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.
Files in this Data Supplement: