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Figure 6.
Crystal structures of caspase-3 in complexes with inhibitors.
A, a ribbon diagram shows the overall structure of caspase-3. B,
molecular surface maps represent the hydrophobic pocket with the
bound inhibitors. C, a stereo view shows the composition of the
hydrophobic pocket at the dimer interface and the oxidation of
the catalytic cysteine (Cys^163) to sulfonic acid. D, the four
inhibitors are superimposed at the binding site within bound
compounds I, II, III, and IV colored in magenta, green, cyan,
and yellow, respectively. E, a stereo view shows the catalytic
active site of molecule C. The 2F[o] - F[c] sa_omit_map (1σ
contour level) for the oxidized catalytic cysteine and the
residues nearby are shown with cyan meshes.
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