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Figure 6.
Figure 6. Effects of the mutation V82A on the
inhibitor-binding mode. The inhibitor subsite P1/P1′ is shown
in ball-and-stick representation along with the pocket S1/S1′
in stick representation, for the structures Bwt (red) and Bmut
(green). The broken lines represent hydrogen bonds between the
active site aspartate residues and the oxygen of the diol in the
center of the inhibitor, whereas the asterisks mark residues
that belong to chain B. Due to the asymmetric mode of binding of
the inhibitor, the S1′ pocket, occupied by the P1′ phenyl
side-chain, accommodates one hydroxyl of the central diol, which
is indicated by a dotted circle. Whereas there is no significant
modification in the P1 subsite due to V82A mutation (marked with
a square), in the P1′ a rotation of the Phe ring of the
inhibitor is observed. This rotation decreases the number of
interactions between the inhibitor's side-chain and the S1′
pocket, while the interactions are maintained in the S1 pocket.
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