Abstract
AKR1B10 is a recently identified NADP+ dependent aldo–keto reductase. It is strongly over expressed in lung and hepatic carcinomas as well as in colorectal and uterine cancers. AKR1B10 has 71% sequence identity with aldose reductase, the latter plays an important role in diabetic complications. The enzyme also exhibits substrate-specificity and inhibitor-sensitivity similar to aldose reductase. Various aldose reductase inhibitors show induced fit phenomenon in aldose reductase. It is reported that the selective ALR2 inhibitor, zopolrestat, also inhibits wild type AKR1B10. In this study, we have performed the induced fit docking of a few aldose reductase inhibitors in crystal structure of AKR1B10 (i.e., 1ZUA). This study elucidates the binding mode of various aldose reductase inhibitors in AKR1B10 and provides insights for the design of more selective and specific inhibitors.
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