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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
1988-8-18
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pubmed:abstractText |
The stoichiometric complex formed between human leukocyte elastase and a synthetic MeO-Suc-Ala-Ala-Pro-Val chloromethyl ketone inhibitor was co-crystallized and its X-ray structure determined, using Patterson search methods. Its structure has been crystallographically refined to a final R value of 0.145 (8.0 and 2.3 A). The enzyme structure is very similar to that recently observed in a complex formed with the ovomucoid third domain from turkey [(1986) EMBO J. 5,2453-2458]. The rms deviation of all alpha-carbon atoms is 0.32 A. The peptidic inhibitor is bound in a similar overall conformation as the ovomucoid binding segment. Covalent bonds are formed between Val-P1 of the inhibitor and His-57 NE2 and Ser-195 OG of the enzyme. The carbonyl carbon is tetrahedrally deformed to a hemiketal. The valine side chain is arranged in the S1 pocket in the g-conformation.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0014-5793
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
18
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pubmed:volume |
234
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
367-73
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:3391280-Amino Acid Chloromethyl Ketones,
pubmed-meshheading:3391280-Amino Acid Sequence,
pubmed-meshheading:3391280-Animals,
pubmed-meshheading:3391280-Binding Sites,
pubmed-meshheading:3391280-Humans,
pubmed-meshheading:3391280-Leukocytes,
pubmed-meshheading:3391280-Models, Molecular,
pubmed-meshheading:3391280-Pancreatic Elastase,
pubmed-meshheading:3391280-Protein Binding,
pubmed-meshheading:3391280-Protein Conformation,
pubmed-meshheading:3391280-X-Ray Diffraction
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pubmed:year |
1988
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pubmed:articleTitle |
The refined 2.3 A crystal structure of human leukocyte elastase in a complex with a valine chloromethyl ketone inhibitor.
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pubmed:affiliation |
Max-Planck-Institut für Biochemie, Martinsried, FRG.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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