Skip to main content
. 2011 Apr 13;286(23):20736–20745. doi: 10.1074/jbc.M111.230367

FIGURE 2.

FIGURE 2.

Comparison of the binding modes of 1-AG and AA in the cyclooxygenase channel. A, stereo view of 1-AG bound in a “productive” conformation in monomer B (dark blue) versus 1-AG bound in a nonoptimal conformation in monomer A (pink) of the muCOX-2:1AG crystal structure. The ω-end of 1-AG does not protrude completely into the hydrophobic groove above Ser-530 in monomer A, resulting in the misalignment of carbon 13. B and C, stereo views of the superposition of the productive conformation of AA (yellow) from monomer B of the muCOX-2:AA crystal structure (10) with the conformation of 1-AG from monomer A (B) and monomer B (C) of the muCOX-2:1AG crystal structure. Cyclooxygenase channel residues in the muCOX2:1AG crystal structure are shown in green and labeled accordingly, whereas the position of Leu-531 in monomer B of the muCOX2:AA crystal structure is shown in yellow. Nitrogen atoms are shown in blue, and oxygen atoms are in red.