Sawaya, M.R.Verma, M.Balendiran, V.Rath, N.P.Cascio, D.Balendiran, G.K.2018-01-052024-08-132018-01-052024-08-1320162016Sawaya, M. R., Verma, M., Balendiran, V., Rath, N. P., Cascio, D., & Balendiran, G. K. (2016). Characterization of WY 14,643 and its complex with Aldose reductase. Scientific Reports, 6. doi: 10.1038/srep34394Online- 2045-23222045232210.1038/srep34394https://kr.cup.edu.in/handle/32116/489The peroxisome proliferator, WY 14,643 exhibits a pure non-competitive inhibition pattern in the aldehyde reduction and in alcohol oxidation activities of human Aldose reductase (hAR). Fluorescence emission measurements of the equilibrium dissociation constants, Kd, of oxidized (hAR? NADP+) and reduced (hAR? NADPH) holoenzyme complexes display a 2-fold difference between them. Kd values for the dissociation of WY 14,643 from the oxidized (hAR? NADP+ ? WY 14,643) and reduced (hAR? NADPH? WY 14,643) ternary complexes are comparable to each other. The ternary complex structure of hAR? NADP+ ? WY 14,643 reveals the first structural evidence of a fibrate class drug binding to hAR. These observations demonstrate how fibrate molecules such as WY 14,643, besides being valued as agonists for PPAR, also inhibit hAR. ? The Author(s) 2016.enAldehyde ReductaseHoloenzymeNicotinamide Adenine Dinucleotide PhosphatePirinixic AcidPyrimidine DerivativeChemistryHumanProtein DomainAldehyde ReductaseHoloenzymesHumansNadpProtein DomainsPyrimidinesArticlehttps://www.nature.com/articles/srep34394