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2.
Figure 4

Figure 4. From: A screening strategy for trapping the inactive conformer of a dimeric enzyme with a small molecule inhibitor.

The 96—well plate arrangement. Positive (+) and negative (−) controls are located in columns 1 and 2 respectively. Test compounds are screened in columns 3—12. The wells in each row receive substrate at the same time. The controls in each row may be used to accurately calculate % inhibition.

Charles S. Craik, et al. Methods Mol Biol. 2012;928:119-131.
3.

Figure 1. From: A screening strategy for trapping the inactive conformer of a dimeric enzyme with a small molecule inhibitor.

KSHV Pr dimer. The top and side views of the dimeric crystal structure are shown. The active—site catalytic residues are in orange. The interfacial α—helix 5 moieties and the two independent catalytic triads are highlighted in black.

Charles S. Craik, et al. Methods Mol Biol. 2012;928:119-131.
4.
Figure 2

Figure 2. From: A screening strategy for trapping the inactive conformer of a dimeric enzyme with a small molecule inhibitor.

The workflow for identifying dimer disruptors of HHV proteases. Inhibitors of KSHV Pr activity are identified by high throughput screening (HTS) of small molecule libraries. Hits are further characterized for mode of inhibition and dimer disruption through 2D—NMR assays that have been described previously. Lead compounds are then tested for efficacy against other HHV proteases. This method will focus on the HTS assay (dotted box).

Charles S. Craik, et al. Methods Mol Biol. 2012;928:119-131.

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