Structure‐based identification of dual ligands at the a2ar and pde10a with anti‐proliferative effects in lung cancer cell‐lines

HIGHLIGHTS

• who: Leen Kalash from the Based on a structural analysis of the available A ­ AR crystal structures, the distance between the α-carbons of ­Val, in , and ­Leu, in , was selected for investigation as a conformational descriptor for receptor activationThe two A ­ AR co-crystallized structures (PDB IDs: , and YDO), which exhibited the largest difference in α-carbon distances between V ­ al, in , and L ­ eu, in , (12., Å versusÅ respectively), were selected for molecular dynamics simulation. Subsequently, compounds, , and , that were docked into the orthosteric site of the inactive form of the ­A AR protein crystal structure (PDB ID . . .
  

   

  

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