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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
29
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pubmed:dateCreated |
1997-8-18
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pubmed:databankReference | |
pubmed:abstractText |
The regulation of cardiac muscle contraction must differ from that of skeletal muscles to effect different physiological and contractile properties. Cardiac troponin C (TnC), the key regulator of cardiac muscle contraction, possesses different functional and Ca2+-binding properties compared with skeletal TnC and features a Ca2+-binding site I, which is naturally inactive. The structure of cardiac TnC in the Ca2+-saturated state has been determined by nuclear magnetic resonance spectroscopy. The regulatory domain exists in a "closed" conformation even in the Ca2+-bound (the "on") state, in contrast to all predicted models and differing significantly from the calcium-induced structure observed in skeletal TnC. This structure in the Ca2+-bound state, and its subsequent interaction with troponin I (TnI), are crucial in determining the specific regulatory mechanism for cardiac muscle contraction. Further, it will allow for an understanding of the action of calcium-sensitizing drugs, which bind to cardiac TnC and are known to enhance the ability of cardiac TnC to activate cardiac muscle contraction.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Alanine,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Troponin C,
http://linkedlifedata.com/resource/pubmed/chemical/Valine
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
18
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pubmed:volume |
272
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
18216-21
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9218458-Alanine,
pubmed-meshheading:9218458-Animals,
pubmed-meshheading:9218458-Binding Sites,
pubmed-meshheading:9218458-Calcium,
pubmed-meshheading:9218458-Chickens,
pubmed-meshheading:9218458-Cloning, Molecular,
pubmed-meshheading:9218458-Escherichia coli,
pubmed-meshheading:9218458-Models, Molecular,
pubmed-meshheading:9218458-Models, Structural,
pubmed-meshheading:9218458-Molecular Sequence Data,
pubmed-meshheading:9218458-Muscle, Skeletal,
pubmed-meshheading:9218458-Mutagenesis, Site-Directed,
pubmed-meshheading:9218458-Myocardium,
pubmed-meshheading:9218458-Point Mutation,
pubmed-meshheading:9218458-Protein Structure, Secondary,
pubmed-meshheading:9218458-Recombinant Proteins,
pubmed-meshheading:9218458-Troponin C,
pubmed-meshheading:9218458-Valine
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pubmed:year |
1997
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pubmed:articleTitle |
Structure of cardiac muscle troponin C unexpectedly reveals a closed regulatory domain.
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pubmed:affiliation |
Department of Biochemistry, Medical Research Council Group in Protein Structure and Function, University of Alberta, Edmonton, Alberta T6G 2H7, Canada.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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