Fig. 2. rCeEI-4 in Bioengineering of an elastase inhibitor from Caesalpinia echinata (Brazil wood) seeds

Fig. 2. rCeEI-4 and rCeEI-5 amino acid sequences and molecular models. (A) Multiple alignment of rCeEI-4 and rCeEI-5 amino acid sequences with other Kunitz type inhibitors. Protein Data Base (PDB) codes are shown in the figure. 1avw_B: trypsin inhibitor from Glycine max; 1tie_A: trypsin inhibitor from Erythrina caffra seeds; 1eyl_A: winged bean chymotrypsin inhibitor; 4an6_B: trypsin inhibitor from Tamarindus indica; 4j2k_B: trypsin inhibitor from Enterolobium contortisiliquum; rCeEI-4 and rCeEI-5: putative elastase inhibitors from C. echinata. The cysteine residues are in black boxes. Residues at P1 and P1′ positions of the putative reactive site are in blue boxes. The Weblogo shows the consensus among the sequences. Theoretical models of (B) rCeEI-4 and (C) rCeEI-5. In both models the beta sheet is shown in red, turns in green, coils in cyan, cysteines involved in the disulfide bonds are in yellow and the putative reactive site in grey. The figures were obtained by the YASARA program. (D) Structural alignment of rCeEI-4 (blue) and rCeEI-5 (green) theoretical models. The disulfide bonds are shown in yellow and putative reactive sites in cyan. (For interpretation of the references to colour in this figure legend, the reader is referred to the Web version of this article.)