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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
16
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pubmed:dateCreated |
1999-10-14
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pubmed:abstractText |
X-ray crystal structure analysis of FR901277, a novel inhibitor of human leukocyte elastase, was performed and revealed that the lipophilic side chains are located towards the outside of the molecule. Binding simulation using computational methods showed that these lipophilic moieties could bind to the hydrophobic binding pockets of HLE.
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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 |
Aug
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pubmed:issn |
0960-894X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
16
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pubmed:volume |
9
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
2397-402
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pubmed:dateRevised |
2004-11-17
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pubmed:meshHeading |
pubmed-meshheading:10476876-Amides,
pubmed-meshheading:10476876-Binding Sites,
pubmed-meshheading:10476876-Crystallography, X-Ray,
pubmed-meshheading:10476876-Enzyme Inhibitors,
pubmed-meshheading:10476876-Humans,
pubmed-meshheading:10476876-Leukocyte Elastase,
pubmed-meshheading:10476876-Models, Molecular,
pubmed-meshheading:10476876-Molecular Structure,
pubmed-meshheading:10476876-Protein Binding
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pubmed:year |
1999
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pubmed:articleTitle |
Molecular structure of FR901277, a novel inhibitor of human leukocyte elastase, and its binding mode simulation.
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pubmed:affiliation |
Basic Research Laboratories, Fujisawa Pharmaceutical Co., Ltd., Osaka, Japan.
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pubmed:publicationType |
Journal Article
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