Novel Hypoxanthine Guanine Phosphoribosyltransferase Gene Mutations in Saudi Arabian Hyperuricemia Patients

Figure 2

(a) Ribbon diagram of HPRT protein showing all the four side chains A, B, C, and D. (b) Location of mutations (K103 M and V160G) identified in the HPRT protein of hyperuricemia patients. (c) Structure of human hypoxanthine guanine phosphoribosyltransferase A-chain displaying K103 M and V160G mutations. (d) Stability change of the mutant calculated by ProSA server. (e) Molecular dynamics (MD) simulation showing truncated octahedron boundary explicit water solvated and hydrogen atoms. The visual inspection also allows identifying the side chain of histidine residues (HSD1–HSD4) involved in hydrogen bonding with the surrounding molecules. (f) HPRT structure superimposed with wild and mutant residues with mutations K103 M and V160G enlarged (g). (h) Change in the protein stability for the observed mutations.