1epp

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{{STRUCTURE_1epp| PDB=1epp | SCENE= }}
{{STRUCTURE_1epp| PDB=1epp | SCENE= }}
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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'''
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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===
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==Overview==
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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.
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==About this Structure==
==About this Structure==
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[[Category: Cooper, J B.]]
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[[Category: Wallace, B A.]]
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Revision as of 22:33, 30 June 2008

Image:1epp.png

Template:STRUCTURE 1epp

ANALYSES OF LIGAND BINDING IN FIVE ENDOTHIAPEPSIN CRYSTAL COMPLEXES AND THEIR USE IN THE DESIGN AND EVALUATION OF NOVEL RENIN INHIBITORS

Template:ABSTRACT PUBMED 8254610

About this Structure

1EPP is a Single protein structure. 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

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