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Figure 1 | BMC Chemical Biology

Figure 1

From: Identification Of Small Molecule TRABID Deubiquitinase Inhibitors By Computation-Based Virtual Screen

Figure 1

TRABID DUB activity assays and structural modeling of TRABID OTU domain. A) Sequence alignment of TRABID OTU domain and A20 OTU domain, the identical (yellow) and homologous (green) pairs are highlighted. B,C) Cleavage of K63 Chains by Recombinant TRABID. Hexa-K63 ubiquitin (0.01 ug/ul) were incubated with recombinant full length TRABID protein prepared from bacteria (B) or Flag-TRABID or Flag-TRABID-C443S precipitated by anti-FLAG agarose from transfected HEK293T cells (C) for 3 hrs in the DUB reaction buffer. Samples were analyzed by Western under a non-reducing condition using an anti-ubiquitin antibody. D-F) Modeled structure of TRABID OTU domain based on the crystal structure of A20 OTU domain. The modeled catalytic site of TRABID OTU domain is shown in D. The detected potential pocket of TRABID OTU domain is shown in E and the corresponding pocket in A20 is shown in F for comparison. The modeled Cys443 is highlighted in sphere representation in E and F.

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BMC Chemical Biology

ISSN: 1472-6769