Linked Life Data

2279290

Source:http://linkedlifedata.com/resource/pubmed/id/2279290

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
1991-3-13
pubmed:abstractText
The crystal of bovine trypsin complexed with a potent inhibitor, 4-[4-(N,N- dimethylcarbamoylmethoxycarbonylmethyl)phenoxycarbonylphenyl ]guanidinium (FOY-305) in the novel orthorhombic from with a low molecular packing density was studied by the X-ray diffraction method. Using synchrotron radiation, the intensity data were collected to 1.8 A resolution. The structure was solved by molecular replacement methods, and refined to an R-factor = 18.0% for 14364 reflections by the restrained least-squares method. The final difference Fourier maps revealed that hydrolyzed inhibitor fragments bind with the protein at multiple sites around the active center of trypsin. The structural feature in the crystalline state probably corresponds to a statistical average of several complexes which would be formed between the inhibitor and trypsin during the binding and releasing process in solution.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0009-2363
pubmed:author
pubmed:issnType
Print
pubmed:volume
38
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2253-5
pubmed:dateRevised
2003-11-14
pubmed:meshHeading
pubmed:year
1990
pubmed:articleTitle
Multiple binding of inhibitors in the complex formed by bovine trypsin and fragments of a synthetic inhibitor, 4-[4-(N,N- dimethylcarbamoxylmethoxycarbonylmethyl)phenoxycarbonylphenyl+ ++] guanidinium methanesulfonate (FOY-305).
pubmed:affiliation
Faculty of Pharmaceutical Sciences, Kyoto University, Japan.
pubmed:publicationType
Journal Article