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Conformations of the regulatory domain of cardiac troponin C examined by residual dipolar couplings

Pääkkönen, Kimmo; Sorsa, Tia; Drakenberg, Torbjörn LU ; Pollesello, Piero; Tilgmann, Carola LU ; Permi, Perttu; Heikkinen, Sami; Kilpeläinen, Ilkka and Annila, Arto (2000) In European Journal of Biochemistry 267(22). p.6665-6672
Abstract

Conformations of the regulatory domain of cardiac troponin C (cNTnC) were studied by means of residual dipolar couplings measured from samples dissolved in dilute liquid crystals. Changes in the main chain HN residual dipolar couplings revealed a conformational change in cNTnC due to the complexation with the second binding region (amino acids 148-163) of cardiac troponin I (cTnI). Formation of the complex is accompanied with a molecular realignment in the liquid crystal. The residual dipolar couplings measured for apo-cNTnC and the complex with TnI were in agreement with the values computed from the corresponding closed and open solution structures, whereas for the calcium-loaded conformation the correlation and quality factor were... (More)

Conformations of the regulatory domain of cardiac troponin C (cNTnC) were studied by means of residual dipolar couplings measured from samples dissolved in dilute liquid crystals. Changes in the main chain HN residual dipolar couplings revealed a conformational change in cNTnC due to the complexation with the second binding region (amino acids 148-163) of cardiac troponin I (cTnI). Formation of the complex is accompanied with a molecular realignment in the liquid crystal. The residual dipolar couplings measured for apo-cNTnC and the complex with TnI were in agreement with the values computed from the corresponding closed and open solution structures, whereas for the calcium-loaded conformation the correlation and quality factor were only modest. Ca2+-cNTnC may be subject to conformational exchange. The data support the model that cardiac troponin C functions as a calcium-dependent open-closed switch, such as the skeletal troponin C.

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author
publishing date
type
Contribution to journal
publication status
published
keywords
Calcium-dependent binding, Cardiac troponin, Conformational exchange, NMR, Residual dipolar couplings
in
European Journal of Biochemistry
volume
267
issue
22
pages
8 pages
publisher
Wiley-Blackwell
external identifiers
  • scopus:0033773598
ISSN
0014-2956
DOI
10.1046/j.1432-1327.2000.01763.x
language
English
LU publication?
no
id
a42bde40-b6a6-4ed9-9843-5d229af63b8b
date added to LUP
2016-04-11 13:16:00
date last changed
2017-02-03 13:15:10
@article{a42bde40-b6a6-4ed9-9843-5d229af63b8b,
  abstract     = {<p>Conformations of the regulatory domain of cardiac troponin C (cNTnC) were studied by means of residual dipolar couplings measured from samples dissolved in dilute liquid crystals. Changes in the main chain HN residual dipolar couplings revealed a conformational change in cNTnC due to the complexation with the second binding region (amino acids 148-163) of cardiac troponin I (cTnI). Formation of the complex is accompanied with a molecular realignment in the liquid crystal. The residual dipolar couplings measured for apo-cNTnC and the complex with TnI were in agreement with the values computed from the corresponding closed and open solution structures, whereas for the calcium-loaded conformation the correlation and quality factor were only modest. Ca<sup>2+</sup>-cNTnC may be subject to conformational exchange. The data support the model that cardiac troponin C functions as a calcium-dependent open-closed switch, such as the skeletal troponin C.</p>},
  author       = {Pääkkönen, Kimmo and Sorsa, Tia and Drakenberg, Torbjörn and Pollesello, Piero and Tilgmann, Carola and Permi, Perttu and Heikkinen, Sami and Kilpeläinen, Ilkka and Annila, Arto},
  issn         = {0014-2956},
  keyword      = {Calcium-dependent binding,Cardiac troponin,Conformational exchange,NMR,Residual dipolar couplings},
  language     = {eng},
  number       = {22},
  pages        = {6665--6672},
  publisher    = {Wiley-Blackwell},
  series       = {European Journal of Biochemistry},
  title        = {Conformations of the regulatory domain of cardiac troponin C examined by residual dipolar couplings},
  url          = {http://dx.doi.org/10.1046/j.1432-1327.2000.01763.x},
  volume       = {267},
  year         = {2000},
}