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Document VII. Conclusions Page 243 The observation of a protein undergoing a conformational change when binding to an inhibitor, as seen with ALR2 and zopolrestat, illustrates a common problem associated with structure-based drug design. It is tempting to view proteins as static structures since their crystal structures are static. Attempts to design drugs to fit the apparent active site of an enzyme may fail when the plasticity of the protein is not taken into account. While the disorder associated with amino acid side chains can be modeled with a moderate computational effort, larger conformational changes—such as the loop movement seen in ALR2—are virtually impossible to predict. Until this becomes possible, x-ray crystal structures of complexes will continue to be indispensible. Finally, it can be easy to forget that a compound's affinity for the protein is not the only consideration when designing inhibitors of enzymes from a structural point of view. The structures of aldose reductase and the FR-1 protein complexed with the drug zopolrestat, a compound with a very high affinity for ALR2, can serve as a reminder of how specificity can also be a very important factor. This is particularly true when a protein is a member of a family of proteins that share sequence homology and are apt to have overlapping specificities. Structure may then play a key role in the determination of features that are unique to the target protein and therefore prime considerations when designing inhibitors. Acknowledgments We thank T. Reynolds who assisted with the production of the figures. This work was supported by a grant from Research to Prevent Blindness, Inc. and grants EY05856, EY02687, and DK20579 to J. Mark Petrash. Florante A. Quiocho is an investigator of the Howard Hughes Medical Institute. References 1. Kinoshita JH, Nishimura C. The involvement of aldose reductase in diabetic complications. Diabetes- Metebolism Rev 1988; 4:323–337. http://legacy.netlibrary.com/nlreader/nlReader.dll?bookid=12640&filename=Page_243.html (1 of 2) [4/5/2004 5:09:27 PM]
Document 2. Lee AYW, Chung SK, Chung SSM. Demonstration that polyol accumulation is responsible for diabetic cataract by the use of transgenic mice expressing the aldose reductase gene in the lens. Proc Natl Acad Sci USA 1995;92:2780–2784. 3. Yamaoka T, Nishimura C, Yamashita K, Itakura M, Yamada T, Fujimoto J, Kokai Y. Acute onset of diabetic pathological changes in transgenic mice with human aldose reductase cDNA. Diabetologia 1995;38:255–261. 4. Sarges R, Oates P. Aldose reductase inhibitors: Recent developments. Prog Drug Res 1993; 40:99–161. http://legacy.netlibrary.com/nlreader/nlReader.dll?bookid=12640&filename=Page_243.html (2 of 2) [4/5/2004 5:09:27 PM]
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