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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
26
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pubmed:dateCreated |
2003-7-1
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pubmed:abstractText |
13C[(15)N] and (13)C[(19)F] rotational-echo double-resonance NMR have been used to characterize the enzyme-bound structure of ZK-816042, an amidine-imidazoline inhibitor of human factor Xa (FXa). The NMR experiments were performed on a lyophilized FXa-inhibitor complex. The complex was formed in solution in the presence of stabilizing excipients and frozen after gradual supercooling prior to lyophilization. The results indicate that the inhibitor binds with a distribution of orientations of the imidazoline ring.
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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 |
0006-2960
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
8
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pubmed:volume |
42
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
7942-9
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:12834346-Amidines,
pubmed-meshheading:12834346-Binding Sites,
pubmed-meshheading:12834346-Factor Xa,
pubmed-meshheading:12834346-Humans,
pubmed-meshheading:12834346-Imidazoles,
pubmed-meshheading:12834346-Magnetic Resonance Spectroscopy,
pubmed-meshheading:12834346-Models, Molecular,
pubmed-meshheading:12834346-Molecular Conformation,
pubmed-meshheading:12834346-Pyridines,
pubmed-meshheading:12834346-Trypsin
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pubmed:year |
2003
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pubmed:articleTitle |
Conformation of a bound inhibitor of blood coagulant factor Xa.
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pubmed:affiliation |
Department of Chemistry, Washington University, St. Louis, Missouri 63130, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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