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Document Figure 7 Schematic illustration of the voids between enzyme and inhibitor in the crystal structure of human renin complexed with a norstatine inhibitor. The figure was produced using the GapE software (Dr. Roman Laskowski). The inhibitor (dark bonds) is enclosed by a net surface and the gaps (where the enzyme and inhibitor are not in contact) are represented by solid surfaces [42]. Page 338 demonstrate the need for careful, high-resolution x-ray analyses for more confidence in drug design. In particular, they show that even minor alternations in the positions of secondary structural elements can lead to major changes in the disposition of the subsites and thus the recognition of substrates. Since such molecular recognition defines the species specificity and determines the catalytic efficiency of the enzymes, a through understanding is indispensable for the synthesis of suitable inhibitors. The specificity pockets—the molecular recognition sites—are modified by elaboration, particularly of surface loops, which can be disordered in the uncomplexed enzymes and difficult to model with precision from homologous structures. These data establish a new foundation for the rational design of renin inhibitors and have provided a rational base for development of clinically successful HIV proteinase inhibitors. References 1. Ondetti MA, Cushman DW. Enzymes of the renin-angiotensin system and their inhibitors. Annu Rev Biochem 1982; 51:283–308. http://legacy.netlibrary.com/nlreader/nlReader.dll?bookid=12640&filename=Page_338.html (1 of 2) [4/5/2004 5:27:09 PM]
Document 2. Blundell TL, Cooper J, Foundling SI, Jones DM, Atrash B, Szelke M. On the rational design of renin inhibitors: X-ray studies of aspartic proteinases complexed with transition state analogues. Biochemistry 1987; 26:5585–5590. http://legacy.netlibrary.com/nlreader/nlReader.dll?bookid=12640&filename=Page_338.html (2 of 2) [4/5/2004 5:27:09 PM]
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Page 421 and 422: Document Page 343 14 Structural Asp
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