Acta Cryst. (2002). D58, 622-626 [doi:10.1107/S0907444902002378]
Abstract: 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-![[bold pi]](/logos/entities/pi_bdgif.gif)
interaction in the native holoenzyme. As a result, the benzene ring of the inhibitor and these side chains form a CH-- interaction. Such structural information is key to understanding the mode of action of this class of inhibitors and for rational design of better therapeutics.
PDB reference: 1iei
Online 22 March 2002
 |   PDF file (184.9 kbytes) |
To open or display or play some files, you may need to set your browser up to use the appropriate software. See the full list of file types for an explanation of the different file types and their related mime types and, where available links to sites from where the appropriate software may be obtained.
The download button will force most browsers to prompt for a file name to store the data on your hard disk.
Where possible, images are represented by thumbnails.
Copyright © International Union of Crystallography
IUCr Webmaster