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- W35274597 abstract "Tolrestat is known to bind tightly (IC50 < 10−7 M) to aldose reductase (E. C. 1. 1. 1. 21; ALR2), enzyme which has been linked to diabetic complications (Kinoshita, 1986; Dvornik, 1987; Kador, 1988). Recently, it has been reported that tolrestat co-crystallizes at the ace site of pig lens ALR2 (Urzhumtsev et al., 1997) and aldehyde reductase (El- Kabbani al., 1997). The reported crystal structure of ALR2 complexed with NADP+ and tolrestat reveals that the carboxylate of tolrestat is hydrogen bonded to Tyr48, His 110 and Trp 111 while the aromatic portion is surrounded by the hydrophobic residues such as Trp20,p219, Trp111, Phe122, and Leu300. The observed hydrogen bonding interaction between tolrestat and ALR2 is essentially identical to that reported in the crystal structure of ALR2 complexed with zopolrestat (Wilson et al. 1993; Wilson et al. 1995). This similarity in hyden bonding interaction indicates that hydrogen bonding or charge interaction between ALR2 and the ionized portion of inhibitors plays an important role in enhancing the binding affinity of inhibitors (Lee et al., 1998)." @default.
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- W35274597 date "1999-01-01" @default.
- W35274597 modified "2023-09-23" @default.
- W35274597 title "Rotamers of Tolrestat and Their Binding Mode to Aldose Reductase" @default.
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- W35274597 doi "https://doi.org/10.1007/978-1-4615-4735-8_58" @default.
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