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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
28
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pubmed:dateCreated |
1993-11-24
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pubmed:abstractText |
One- and two-dimensional NMR techniques were used to compare the structural consequences of Ca2+ binding to both the low and high affinity Ca2+ binding sites in recombinant cardiac troponin C (cTnC3). In the absence of Ca2+, the short beta-sheet located between the high affinity Ca2+/Mg2+ binding sites in the C-terminal domain was found to be absent or loosely formed as judged by the inter-residue NOEs and chemical shifts of resonances in the Ca2+ binding loops. In contrast, the N-terminal domain beta-sheet located between site II and the naturally inactive site I was present even in the absence of bound Ca2+. Calcium-binding mutant proteins having either an inactive Ca2+ binding site III (CBM-III) or an inactive Ca2+ binding site IV (CBM-IV) (Negele, J. C., Dotson, D., Liu, W., Sweeney, H. L., and Putkey, J. A. (1992) J. Biol. Chem. 267, 825-831) were used to study the structural consequences of Ca2+ binding to each of the high affinity sites located in the C-terminal domain. Only a single active Ca2+ binding site was found necessary for formation of the short beta-sheet between Ca2+ binding sites III and IV. However, the absence of bound Ca2+ at site III was found to produce greater instability in the C-terminal domain as judged from the mobility of the C-terminal aromatic hydrophobic cluster. Thus, Ca2+ binding to the high affinity sites in the C-terminal domain results in an ordering of the aromatic hydrophobic cluster, as well as formation of a short beta-sheet between Ca2+ binding sites III and IV. These results demonstrate that Ca2+ binding plays distinctive structural roles in the N- and C-terminal domains of cTnC.
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pubmed:grant | |
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 |
Oct
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
5
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pubmed:volume |
268
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
20966-73
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:8407932-Binding Sites,
pubmed-meshheading:8407932-Calcium,
pubmed-meshheading:8407932-Magnetic Resonance Spectroscopy,
pubmed-meshheading:8407932-Metals,
pubmed-meshheading:8407932-Myocardium,
pubmed-meshheading:8407932-Protein Conformation,
pubmed-meshheading:8407932-Troponin,
pubmed-meshheading:8407932-Troponin C
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pubmed:year |
1993
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pubmed:articleTitle |
Calcium plays distinctive structural roles in the N- and C-terminal domains of cardiac troponin C.
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pubmed:affiliation |
Department of Biochemistry and Molecular Biology, University of Texas Medical School, Houston 77225.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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