ArticleProceedings of the National Academy of Sciences of the United States of America2002
Structure of the inhibitory region of troponin by site directed spin labeling electron paramagnetic resonance.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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24 citing papers in PubMed.
- Structural Dynamics of the N-Extension of Cardiac Troponin I Complexed with Troponin C by Site-Directed Spin Labeling Electron Paramagnetic Resonance.Scientific reports · 2019Article
- Constructing a structural model of troponin using site-directed spin labeling: EPR and PRE-NMR.Biophysical reviews · 2019Review
- Cardiac troponin structure-function and the influence of hypertrophic cardiomyopathy associated mutations on modulation of contractility.Archives of biochemistry and biophysics · 2016Review
- Ca(2+)-regulatory function of the inhibitory peptide region of cardiac troponin I is aided by the C-terminus of cardiac troponin T: Effects of familial hypertrophic cardiomyopathy mutations cTnI R145G and cTnT R278C, alone and in combination, on filament sliding.Archives of biochemistry and biophysics · 2014Article
- Ca2+-induced PRE-NMR changes in the troponin complex reveal the possessive nature of the cardiac isoform for its regulatory switch.PloS one · 2014Article
- Interdomain orientation of cardiac troponin C characterized by paramagnetic relaxation enhancement NMR reveals a compact state.Protein science : a publication of the Protein Society · 2012Article
- pH-responsive titratable inotropic performance of histidine-modified cardiac troponin I.Biophysical journal · 2012Article
- Global structure of a three-way junction in a phi29 packaging RNA dimer determined using site-directed spin labeling.Journal of the American Chemical Society · 2012Article
- RosettaEPR: an integrated tool for protein structure determination from sparse EPR data.Journal of structural biology · 2011Article
- Low temperature dynamic mapping reveals unexpected order and disorder in troponin.The Journal of biological chemistry · 2010Article
- Dual regulatory functions of the thin filament revealed by replacement of the troponin I inhibitory peptide with a linker.The Journal of biological chemistry · 2010Article
- Switch action of troponin on muscle thin filament as revealed by spin labeling and pulsed EPR.The Journal of biological chemistry · 2010Article
- Distance and dynamics determination by W-band DEER and W-band ST-EPR.European biophysics journal : EBJ · 2010Article
- Troponin regulatory function and dynamics revealed by H/D exchange-mass spectrometry.The Journal of biological chemistry · 2010Article
- The myosin-binding protein C motif binds to F-actin in a phosphorylation-sensitive manner.The Journal of biological chemistry · 2009Article
- Conformational changes at the tetramerization site of erythroid alpha-spectrin upon binding beta-spectrin: a spin label EPR study.Biochemistry · 2008Article
- Interaction of cardiac troponin with cardiotonic drugs: a structural perspective.Biochemical and biophysical research communications · 2008Review
- Applications of electron paramagnetic resonance to studies of neurological disease.European biophysics journal : EBJ · 2008Review
- De novo high-resolution protein structure determination from sparse spin-labeling EPR data.Structure (London, England : 1993) · 2008Article
- Probing protein-peptide binding surfaces using charged stable free radicals and transverse paramagnetic relaxation enhancement (PRE).Journal of biomolecular NMR · 2005Article
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7 authors.
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Abstract
Site-directed spin labeling EPR (SDSL-EPR) was used to determine the structure of the inhibitory region of TnI in the intact cardiac troponin ternary complex. Maeda and collaborators have modeled the inhibitory region of TnI (skeletal 96-112: the structural motif that communicates the Ca(2+) signal to actin) as a kinked alpha-helix [Vassylyev, D., Takeda, S., Wakatsuki, S., Maeda, K. & Maeda, Y. (1998) Proc. Natl. Acad. Sci. USA 95, 4847-4852), whereas Trewhella and collaborators have proposed the same region to be a flexible beta-hairpin [Tung, C. S., Wall, M. E., Gallagher, S. C. & Trewhella, J. (2000) Protein Sci. 9, 1312-1326]. To distinguish between the two models, residues 129-145 of cardiac TnI were mutated sequentially to cysteines and labeled with the extrinsic spin probe, MTSSL. Sequence-dependent solvent accessibility was measured as a change in power saturation of the spin probe in the presence of the relaxation agent. In the ternary complex, the 129-137 region followed a pattern characteristic of a regular 3.6 residues/turn alpha-helix. The following region, residues 138-145, showed no regular pattern in solvent accessibility. Measurements of 4 intradomain distances within the inhibitory sequence, using dipolar EPR, were consistent with an alpha-helical structure. The difference in side-chain mobility between the ternary (C.I.T) and binary (C.I) complexes revealed a region of interaction of TnT located at the N-terminal end of the inhibitory sequence, residues 130-135. The above findings for the troponin complex in solution do not support either of the computational models of the binary complex; however, they are in very good agreement with a preliminary report of the x-ray structure of the cardiac ternary complex [Takeda, S. Yamashita, A., Maeda, K. & Maeda, Y. (2002) Biophys. J. 82, 832].
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