Dissecting mutational allosteric effects in alkaline phosphatases associated with different Hypophosphatasia phenotypes: An integrative computational investigation
Fig 9
Allosteric effects of three studied severe mutations (N47I, L289F and M355I) and two predicted severe mutations (R391C and E452K) calculated by AlloSigMA.
Cartoon structures of the TNSALP protein colored according to their free energy values obtained for the cases of (A) N47I, (B) L289F, (C) M355I, (D) R391C and (E) E452K, while blue color indicates negative allosteric free energy and red color indicates positive modulation. (F) Their free energy profiles are illustrated graphically with the residue index (chain A: 1–524; chain B: 525–1048) on the x-axis and Δg value on the y-axis. Blue, yellow, green, pink and red profiles represent the results for N47I, L289F, M355I, R391C and E452K, respectively.