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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
15
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pubmed:dateCreated |
2001-7-20
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pubmed:abstractText |
[structure: see text] The design, synthesis, and enzyme inhibition of a new class of aspartic peptidase inhibitors is described. Unsymmetrical ureas were designed from computer-generated structures. Using mechanism-based and substrate-based design techniques, potent pepsin inhibitors were developed and the binding mode was established. Two X-ray crystal structures of enzyme-bound inhibitors revealed a new binding mode that is closely related to the computer-generated binding mode.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
1523-7060
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
26
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pubmed:volume |
3
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2313-6
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:11463304-Animals,
pubmed-meshheading:11463304-Aspartic Acid Endopeptidases,
pubmed-meshheading:11463304-Computer Simulation,
pubmed-meshheading:11463304-Crystallography, X-Ray,
pubmed-meshheading:11463304-Drug Design,
pubmed-meshheading:11463304-Pepsin A,
pubmed-meshheading:11463304-Peptides,
pubmed-meshheading:11463304-Protease Inhibitors,
pubmed-meshheading:11463304-Protein Conformation,
pubmed-meshheading:11463304-Structure-Activity Relationship,
pubmed-meshheading:11463304-Swine,
pubmed-meshheading:11463304-Urea
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pubmed:year |
2001
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pubmed:articleTitle |
Design and synthesis of unsymmetrical peptidyl urea inhibitors of aspartic peptidases.
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pubmed:affiliation |
Department of Chemistry, University of Wisconsin-Madison, 1101 University Avenue, Madison, Wisconsin 53706, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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