FIGURE 3.

Annexin V hinge movement and binding sites of Xe or N₂O. Smooth carbon α-chain representation of annexin V monomer in low- and high-calcium conformation (colored in purple and blue, respectively) showing the hinge movement of the loop carrying the tryptophan 185 in parallel to the glutamate 226 switch. Both Xe and N₂O bind within the hydrophobic cavity left vacant by the movement of the tryptophan. A second molecule of N₂O binds in the center of the first domain. The color code is the same as above plus the calcium colored in pink. Figs. 2 and 3 were produced with the visualization software InsightII (Accelrys, San Diego, CA).