Computational Analysis of nsSNPs of ADA Gene in Severe Combined Immunodeficiency Using Molecular Modeling and Dynamics Simulation

Figure 3

The structural analysis of the different interactions in the mutated protein and the wild-type protein. (a) H15 (wild-type ADA) and 15D (variant protein), (b) H15 (wild-type ADA) and 15P (variant protein), (c) H17 (wild-type ADA) and 17Q (variant protein), (d) H17 (wild-type ADA) and 17Y (variant protein), (e) D19 (wild-type ADA) and 19N (variant protein), (f) T26 (wild-type ADA) and 26I (variant protein), (g) G140 (wild-type ADA) and 140E (variant protein), (h) C153 (wild-type ADA) and 153F (variant protein), (i) A183 (wild-type ADA) and 183D (variant protein), (j) G216 (wild-type ADA) and 216R (variant protein), (k) H258 (wild-type ADA) and 258Y (variant protein), (l) C262 (wild-type ADA) and 262Y (variant protein), (m) S291 (wild-type ADA) and 291L (variant protein), (n) S291 (wild-type ADA) and 291W (variant protein), and (o) K340 (wild-type ADA) and 340E (variant protein). Residues substituted are shown in red; residues involved in hydrogen bonds are marked in magenta; residues that participate in hydrophobic interactions are indicated in cyan; residues that participate in both hydrogen bonds and hydrophobic interactions are marked in yellow; residues which lost hydrogen bonds and/or hydrophobic interactions are marked in blue; and new residues which appeared are indicated in green. Hydrogen bonding is marked by yellow dashed lines, and hydrophobic interactions are shown in green lines.

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