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Figure 4.
Fig. 4. Mode of binding of compactin (A), simvastatin (B),
fluvastatin (C), cerivastatin (D), atorvastatin (E), and
rosuvastatin (F) to human HMGR. Interactions between the HMG
moieties of the statins and the protein are mostly ionic or
polar. They are similar for all inhibitors and are indicated by
the dotted lines. Numbers next to the lines indicate distances
in Å (13). The rigid hydrophobic groups of the statins are
situated in a shallow groove between helices L  1 and L
10.
Additional interactions between Arg590 and the fluorophenyl
group are present in the type 2 statins (C, D, E, F).
Atorvastatin and rosuvastatin form a hydrogen bond between
Ser565 and a carbonyl oxygen atom (atorvastatin) (E) or a
sulfone oxygen atom (rosuvastatin) (F).
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