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Figure 2.
Figure 2. Binding of NU6094, NU6086 and NU6102 to T160pCDK2
-cyclinA. a, T160pCDK2 -cyclinA -NU6094 structure. Selected
CDK2 residues are drawn in ball-and-stick representation, with
carbon atoms colored green (inhibitor) and yellow (CDK2). The
final 2F[o]-F[c] electron density contoured at 0.24 e^- Å-3 for
NU6094 is included. Hydrogen bonds in all panels except (b) are
denoted by dashed lines. b, NU6094 bound to the CDK2 active
site. NU6094 is depicted as yellow CPK spheres. The CDK2
molecular surface is colored by atom type: carbon, oxygen and
nitrogen atoms are green, red and blue, respectively. The figure
illustrates the complementarity of the NU6094 anilino ring to
the shape of the hydrophobic tunnel leading to the specificity
surface. c, T160pCDK2 -cyclinA -NU6086 structure. NU6086 and
selected CDK2 residues are rendered in ball-and
stick-representation, with carbon atoms colored as in (a). Both
conformers of the anilino ring (denoted I and II) are included.
The final 2F[o]-F[c] electron density for NU6086 is contoured at
0.24 e^- Å-3. d, T160pCDK2 -cyclinA -NU6102 structure. NU6102
and selected CDK2 residues are rendered in ball-and-stick
representation, with carbon atoms colored as in (a). The final
2F[o]-F[c] electron density for NU6102 is contoured at 0.24 e^-
Å-3. e, NU6102 bound to the CDK2 active site. The CDK2 molecular
surface is rendered in transparent gray so that interactions
between the NU6102 sulfonamide group and the backbone nitrogen
and side chain oxygen of Asp 86 are visible. Hydrogen bonds are
depicted by dotted lines. NU6102 is rendered in ball and stick,
with carbon atoms colored green.
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