Illustration of the conformational changes occurring in the proteolytic region of the prodomain, solvent-accessible surface area and multiple structure alignments.
<p>(A) Superimposition of the prodomain proteolytic region (top panel) shows significant conformational changes (R51-A70) in the glycosylated in contrast to non-glycosylated proMMP-9. The right top panel represents times-series of the distance between the Cα atoms of E59-R106 in the glycosylated (black) and non-glycosylated (red) proMMP-9, demonstrating the mobility of the loop. The lower left panel represents the glycosylated proMMP-9 prodomain in closed conformation (first cleavage region protects the second one and the distance between them is 10.9 Å). Lower right panel represents the non-glycosylated proMMP-9 prodomain in open conformation (both cleavages regions are exposed and the distance between them is 24.6 Å). (B) Left and right panel represents the solvent-accessible surface area (SASA in Å<sup>2</sup>) of two proteolytic fragments for glycosylated and non-glycosylated form of proMMP-9, respectively. (C) Superimposition of seven snapshots, each at 80ns intervals out of the 500ns MD trajectory. Glycans are represented according to the Consortium For Glycomics nomenclature.</p
