Dissecting mutational allosteric effects in alkaline phosphatases associated with different Hypophosphatasia phenotypes: An integrative computational investigation
Fig 8
Allosteric paths originating at three mutational sites and terminating at S258 in the WT (A) and mutant states (B), as well as terminating at N190 in the WT (C) and mutant states (D), respectively. The TNSALP structure is depicted as represented by a semitransparent colored cartoon, and the starting and ending residues of all the paths are represented as green and cyan spheres, respectively. The alpha-carbon of the path through the residues is shown as silver (chain A) and orange (chain B) spheres, in which active sites are represented by red spheres.