Thermodynamic analysis of morphine enantiomers binding to MOR. (IMAGE)

Science China Press

Thermodynamic analysis of morphine enantiomers binding to MOR.

Caption

(A) Binding energies of (-)-morphine and (+)-morphine interacting with MOR. (B) Binding pocket residues of (-)-morphine and (+)-morphine in MOR, visualized from the extracellular side. (C) W293 flipping into the binding site to establish hydrophobic interactions and stabilize (-)-morphine in the activated MOR. (D) Alignment of (-)-morphine-bound MOR and (+)-morphine-bound MOR with the activated crystal structure of MOR, highlighting the significant conformational changes compared to the activated state.

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