Structural highlights
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Lunney EA, Hamilton HW, Hodges JC, Kaltenbronn JS, Repine JT, Badasso M, Cooper JB, Dealwis C, Wallace BA, Lowther WT, et al.. Analyses of ligand binding in five endothiapepsin crystal complexes and their use in the design and evaluation of novel renin inhibitors. J Med Chem. 1993 Nov 26;36(24):3809-20. PMID:8254610
