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Fig. 6 | Journal of Hematology & Oncology

Fig. 6

From: Allosteric activation of the metabolic enzyme GPD1 inhibits bladder cancer growth via the lysoPC-PAFR-TRPV2 axis

Fig. 6

Discovery of a cellularly active GPD1 allosteric activator. A Crystal structure of GPD1 protein (PDB ID:6E8Y). The potential allosteric sites were predicted using the Allosite server (http://mdl.shsmu.edu.cn/AST/). Red represents the predicted allosteric sites. B Superposition of GPD1 protein with compounds selected by virtual screening. C. The structure and docking score of compounds from Bioactive Compound Library Plus on the basis of the top-ranked GPD1-compound binding models. D Construction and validation of the GPD1 enzyme activity analysis system. E The effect of compounds on the activation of GPD1 enzyme activity was determined by a GPD1 enzyme activity analysis system. F Binding affinity of wedelolactone and GPD1 was measured by MST. G and H Detection of intracellular G3P and NAD+ levels in 5637 and T24 cells treated with wedelolactone

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