| Structures determined by the Macromolecular Crystallography Laboratory, Protein Structure Section at the NCI-Frederick campus. Work performed in collaboration with the Skalka Laboratory in the Institute for Cancer Research, Fox Chase Cancer Center, and with the Laboratory of Molecular Pharmacology and the Laboratory of Medicinal Chemistry, Division of Basic Sciences, NCI, NIH. |
This view shows the inhibitor bound in the vicinity of the ASV IN active site (residues D121, D64, E157). The native structure (1ASV) is shown in purple and the ASV IN-inhibitor complex is shown in green. Two Y-3 inhibitor molecules are shown in yellow and green at the bottom.
A VRML
image, which some web browsers can view and manipulate, is available.
This view shows the inhibitor bound next to the flexible loop, which is involved in substrate binding. There is a significant shift from the structure without Y-3 inhibitor (1ASV, purple) to the ASV IN-inhibitor complex (green).
A VRML image, which some web browsers can view and manipulate, is available.
Note: These inhibitors are not drugs and they are highly toxic. Significant further research must be done in order to increase solubility, increase potency, and reduce toxicity before any chemicals can be considered for human testing or medical use. Many thousands of inhibitors are tested for every one that passes the stringent tests required before an inhibitor can be used as a drug.
Back to the ASV IN Y-3 Inhibitor page.
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