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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 Å 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–π interaction in the native holoenzyme. As a result, the benzene ring of the inhibitor and these side chains form a CH–π–π interaction. Such structural information is key to understanding the mode of action of this class of inhibitors and for rational design of better therapeutics.

Supporting information

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Portable Document Format (PDF) file https://doi.org/10.1107/S0907444902002378/gr2214sup1.pdf
Supplementary material

PDB reference: aldose reductase–zenarestat complex, 1iei, r1ieisf


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