Docking study elucidate the binding mode of Luteolin in the active site of inducible cyclooxygenase-2

Luteolin is one of flavonoids and more precisely one of the citrus bioflavonoids which has antioxidant, anti-inflammatory activity. It is found in high amounts in thyme, basil herb and artichoke. Our aim was to well understand the structural and conformational features responsible for the inhibitory capability of this molecule and illustrate their binding mode in the active site of COX-2 by comparing them with the binding mode of the co-crystallized COX-2 with the SC-558. Therefore a docking study was performed to test the inhibitory of this molecule on COX-2 using Surflex-dock software. The docking results allowed us to provide a possible explanation for the ability of Luteolin to inhibit the COX-2, these results show that Luteolin occupied the region of low affinity and the site SR (side pocket) of the region of high affinity and interact with important conserved residues in particular His90, Gln192, Ile517, Leu352 and Met522 which considered essential for the inhibition and binding of the Luteolin to the active site of COX-2