1epq: Difference between revisions

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[[Image:1epq.~~gif~~|left|200px]]

[[Image:1epq.png|left|200px]]

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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~~'''~~

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

~~==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.~~

The line below this paragraph, {{ABSTRACT_PUBMED_8254610}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 8254610 is the PubMed ID number.

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==About this Structure==

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[[Category: Cooper, J B.]]

[[Category: Dealwis, C.]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ ~~2 15~~:22:55 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 01:33:00 2008''

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-[[Image:1epq.gif|left|200px]]
+{{Seed}}
+[[Image:1epq.png|left|200px]]
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 {{STRUCTURE_1epq|  PDB=1epq  |  SCENE=  }}
-'''ANALYSES OF LIGAND BINDING IN FIVE ENDOTHIAPEPSIN CRYSTAL COMPLEXES AND THEIR USE IN THE DESIGN AND EVALUATION OF NOVEL RENIN INHIBITORS'''
+===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.
+The line below this paragraph, {{ABSTRACT_PUBMED_8254610}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 8254610 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_8254610}}
 ==About this Structure==
@@ Line 25: / Line 29: @@
 [[Category: Cooper, J B.]]
 [[Category: Dealwis, C.]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 15:22:55 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 01:33:00 2008''