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Figure 6 | Parasites & Vectors

Figure 6

From: Isolation and molecular characterization of a major hemolymph serpin from the triatomine, Panstrongylus megistus

Figure 6

Theoretical model of the PMSRP1. A- The structure shows three β-sheets groups (green), nine α-helices (red), the breach (B), shutter (S), gate (G), hinge (H) and the predicted reactive center loop (RCL) regions [61, 62]. A1 shows RCL and the putative residues P17-P9 and P1, P1′, P3′ and P4′ based on alignments. A2 left shows the 40-residue-long C-terminal region (pink) inserted in the structure, and A2 right shows C-terminal interacting with several H-bonds (white dots) helping to maintain a group of β-sheets. B- The serpin molecular surface (top) and the electrostatic potential maps (bottom) showing the distribution of positive (blue) and negative (red) regions on the molecular surface (left front and right back views).

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