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The structure of human recombinant aldose reductase complexed with the potent inhibitor zenarestat.

The crystal structure of the complex of human recombinant aldose reductase ( AR) with zenarestat, one of its potent inhibitors, has been solved at 2.5 A resolution. Zenarestat fits neatly in the hydrophobic active site and induces unique and dramatic conformational changes. For example, the benzene ring of zenarestat occupies a gap in the side chains of Leu300 and Trp111 that interact directly and forms a CH-pi interaction in the native holoenzyme. As a result, the benzene ring of the inhibitor and these side chains form a CH-pi-pi interaction. Such structural information is key to understanding the mode of action of this class of inhibitors and for rational design of better therapeutics.[1]

References

  1. The structure of human recombinant aldose reductase complexed with the potent inhibitor zenarestat. Kinoshita, T., Miyake, H., Fujii, T., Takakura, S., Goto, T. Acta Crystallogr. D Biol. Crystallogr. (2002) [Pubmed]
 
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