Conformations of the regulatory domain of cardiac troponin C examined by residual dipolar couplings
Author
Summary, in English
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.
Publishing year
2000
Language
English
Pages
6665-6672
Publication/Series
European Journal of Biochemistry
Volume
267
Issue
22
Links
Document type
Journal article
Publisher
Wiley-Blackwell
Keywords
- Calcium-dependent binding
- Cardiac troponin
- Conformational exchange
- NMR
- Residual dipolar couplings
Status
Published
ISBN/ISSN/Other
- ISSN: 0014-2956