1bil: Difference between revisions

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[[Image:1bil.jpg|left|200px]]
{{Seed}}
[[Image:1bil.png|left|200px]]


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{{STRUCTURE_1bil|  PDB=1bil  |  SCENE=  }}  
{{STRUCTURE_1bil|  PDB=1bil  |  SCENE=  }}  


'''CRYSTALLOGRAPHIC STUDIES ON THE BINDING MODES OF P2-P3 BUTANEDIAMIDE RENIN INHIBITORS'''
===CRYSTALLOGRAPHIC STUDIES ON THE BINDING MODES OF P2-P3 BUTANEDIAMIDE RENIN INHIBITORS===




==Overview==
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The binding modes of three peptidomimetic P2-P3 butanediamide renin inhibitors have been determined by x-ray crystallography. The inhibitors are bound with their backbones in an extended conformation, and their side chains occupying the S5 to S1' pockets. A (2-amino-4-thiazolyl)methyl side chain at the P2 position shows stronger hydrogen-bonding and van der Waals interactions with renin than the His side chain, which is present in the natural substrate. The ACHPA-gamma-lactam transition state analog has similar interactions with renin as the dihydroxyethylene transition state analog.
The line below this paragraph, {{ABSTRACT_PUBMED_7493993}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 7493993 is the PubMed ID number.
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{{ABSTRACT_PUBMED_7493993}}


==About this Structure==
==About this Structure==
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[[Category: Tong, L.]]
[[Category: Tong, L.]]
[[Category: Aspartic proteinase]]
[[Category: Aspartic proteinase]]
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