Structure-Function of Falcipains: Malarial Cysteine Proteases
Figure 11
(a) Interaction of falcipain-3 with morpholinourea-leucine-homophenylanyl-phenyl vinylsulfone (Mu-Leu-Hph-VsPh). The residues in the active site of falcipain-3 are colored yellow and labeled, and morpholinourea-leucine-homophenylanyl-phenyl vinylsulfone is colored gray. The interactions with enzyme and inhibitor are in black dots. (b) The active site of falcipain-3 with hydrophobic environment. The inhibitor occupies the S1′, S1, S2, S3 subsites of enzyme. Hydrophobic residues are colored light green, and polar residues that interact with the inhibitor by nonpolar C–C bonds are colored dark green [48].
