Title : Effects of ligand binding on the stability of aldo-keto reductases: Implications for stabilizer or destabilizer chaperones.

Pub. Date : 2016 Dec

PMID : 27595938






2 Functional Relationships(s)
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1 Using the differential scanning fluorimetry and the circular dichroism varying the urea concentration and temperature, we found that when the coenzyme NADP+ was absent, inhibitors such as isolithocholic acid stabilized the aldo-keto reductase AKR1A1 upon binding, which showed actually the three-state folding, but destabilized AKR1B10. NADP aldo-keto reductase family 1 member A1 Homo sapiens
2 In contrast, in the presence of NADP+ , they destabilized AKR1A1 and stabilized AKR1B10. NADP aldo-keto reductase family 1 member A1 Homo sapiens