1epp
From Proteopedia
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ANALYSES OF LIGAND BINDING IN FIVE ENDOTHIAPEPSIN CRYSTAL COMPLEXES AND THEIR USE IN THE DESIGN AND EVALUATION OF NOVEL RENIN INHIBITORS
Overview
Five renin inhibitors were cocrystallized with endothiapepsin, a fungal enzyme homologous to renin. Crystal structures of inhibitor-bound complexes have provided invaluable insight regarding the three-dimensional structure of the aspartic proteinase family of enzymes, as well as the steric and polar interactions that occur between the proteins and the bound ligands. Beyond this, subtleties of binding have been revealed, including multiple subsite binding modes and subsite interdependencies. This information has been applied in the design of novel potent renin inhibitors and in the understanding of structure-activity relationships and enzyme selectivities.
About this Structure
1EPP is a Single protein structure of sequence from [1] with , and as ligands. Active as Endothiapepsin, with EC number 3.4.23.22 Full crystallographic information is available from OCA.
Reference
Analyses of ligand binding in five endothiapepsin crystal complexes and their use in the design and evaluation of novel renin inhibitors., Lunney EA, Hamilton HW, Hodges JC, Kaltenbronn JS, Repine JT, Badasso M, Cooper JB, Dealwis C, Wallace BA, Lowther WT, et al., J Med Chem. 1993 Nov 26;36(24):3809-20. PMID:8254610
Page seeded by OCA on Thu Feb 21 12:30:17 2008
