Structure-Function of Falcipains: Malarial Cysteine Proteases

Figure 4

(a) Structure of profalcipain-2: The mature domain (magenta) of falcipain-2 was solved by X-ray diffraction. The active site (catalytic triad residues in orange), refolding domain, and hemoglobin domain are labeled [25]. The prodomain (cyan) modeling was done based on procathepsin L and K [24]. The prodomain runs up the face of the mature enzyme (purple) before forming α helices containing the conserved ERFNIN and GNFD motifs (yellow). Since there is no homology, the 160 N-terminal residues of the prodomain are not included in the prodomain model. (b) Prodomain-mature domain interactions. Closeup of predicted interactions between the mature domain (magenta) and the ERFNIN (R¹⁸⁵) and GNFD (E²¹⁰; F²¹⁴) motifs of prodomain (cyan). Blue dashed lines indicate presumed stabilizing interactions (both electrostatic as well as hydrophobic) between residues [24].

(a)

(b)