X-ray crystallographic analysis of inhibition of endothiapepsin by cyclohexyl renin inhibitors
1992
The crystal structures of endothiapepsin, a fungal aspartic proteinase (EC 3.4.23.6), cocrystallized with two oligopeptide renin inhibitors, PD 125967 and PD 125754, have been determined at 2.0-A resolution and refined to R-factors of 0.143 and 0.153, respectively. These inhibitors, which are of the hydroxyethylene and statine types, respectively, possess a cyclohexylalanine side chain at P 1 and have interesting functionalities at the P 3 position which, until now, have not been subjected to crystallographic analysis
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