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Figure 7.
Fig. 7. Structural changes in the regions around mutations
identified in the third generation. (a) A15S mutation in the
background of F17S mutation makes a hydrogen bond with the same.
(b) Region around mutation A20E showing a water molecule making
hydrogen bonds with side chains of residues Glu20, Ser24 and
Arg33. (c) Electrostatic network consisting of side chains of
Arg107 and Asp144, main-chain carbonyl groups of residues 107
and 142 and three water molecules named WT1, WT2 and WT3 in the
wild-type protein. (d) Immediate vicinity around G111D mutation
showing WT2 is replaced by carboxylate oxygen of Asp111 in the
mutant. Stick representations of loop regions 107–108 and
142–143 are overlaid on the ribbon representations. In all the
figures, water molecules are shown as red spheres and small blue
spheres show electrostatic interactions.
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