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Figure 2.
Fig. 2. Statins exploit the conformational flexibility of HMGR
to create a hydrophobic binding pocket near the active site. (A)
Active site of human HMGR in complex with HMG, CoA, and NADP.
The active site is located at a monomer-monomer interface. One
monomer is colored yellow, the other monomer is in blue.
Selected side chains of residues that contact the substrates or
the statin are shown in a ball-and-stick representation (20).
Secondary structure elements are marked by black labels. HMG and
CoA are colored in magenta; NADP is colored in green. To
illustrate the molecular volume occupied by the substrates,
transparent spheres with a radius of 1.6 Å are laid over
the ball-and-stick representation of the substrates or the
statin. (B) Binding of rosuvastatin to HMGR. Rosuvastatin is
colored in purple; other colors and labels are as in (A). This
figure and Figs. 3 and 4 were prepared with Bobscript (22), GLR
(23), and POV-Ray (24).
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