ArticleProceedings of the National Academy of Sciences of the United States of America2005
Ca(2+)-regulated structural changes in troponin.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 169 papers.
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Who cites it
169 citing papers in PubMed, 306 citations in OpenAlex.
- Troponin: biology, molecular mechanisms, and multidimensional clinical applications.Molecular biomedicine · 2026Review
- Thin filament interaction and CaJournal of molecular and cellular cardiology · 2026Article
- Cardiac Myosin Inhibitors in Hypertrophic Cardiomyopathy: From Sarcomere to Clinic.International journal of molecular sciences · 2025Review
- Intracellular CaBiologia futura · 2025Review
- The highly conserved C-terminal end segment of troponin T binds tropomyosin and actin to function in modulating contractile kinetics.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Structural changes in troponin during activation of skeletal and heart muscle determined in situ by polarised fluorescence.Biophysical reviews · 2024Review
- Variations of VEGFR2 Chemical Space: Stimulator and Inhibitory Peptides.International journal of molecular sciences · 2024Article
- Role of the interaction between troponin T and AMP deaminase by zinc bridge in modulating muscle contraction and ammonia production.Molecular and cellular biochemistry · 2024Review
- Glutamate 139 of tropomyosin is critical for cardiac thin filament blocked-state stabilization.Journal of molecular and cellular cardiology · 2024Article
- Article
- Structure and dynamics of endogenous cardiac troponin complex in human heart tissue captured by native nanoproteomics.Nature communications · 2023Article
- Modulation of Structure and Dynamics of Cardiac Troponin by Phosphorylation and Mutations Revealed by Molecular Dynamics Simulations.The journal of physical chemistry. B · 2023Article
- Recent studies of the molecular mechanism of lusitropy due to phosphorylation of cardiac troponin I by protein kinase A.Journal of muscle research and cell motility · 2023Review
- Zebrafish as a model for cardiac disease; Cryo-EM structure of native cardiac thin filaments from Danio Rerio.Journal of muscle research and cell motility · 2023Article
- Intermolecular And Dynamic Investigation of The Mechanism of Action of Reldesemtiv on Fast Skeletal Muscle Troponin Complex Toward the Treatment of Impaired Muscle Function.The protein journal · 2023Article
- Activation of skeletal muscle is controlled by a dual-filament mechano-sensing mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Distal arthrogryposis in a girl arising from a novel TNNI2 variant inherited from paternal somatic mosaicism.Journal of human genetics · 2023Article
- Conversion of a Cardiac Muscle Modulator from an Inhibitor to an Activator.ACS medicinal chemistry letters · 2023Article
- Cardiac Troponin, Cognitive Function, and Dementia: A Systematic Review.Aging and disease · 2023Review
- Molecular Dynamics Assessment of Mechanical Properties of the Thin Filaments in Cardiac Muscle.International journal of molecular sciences · 2023Article
109 more citing papers are in PubMed but not listed here.
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
Abstract
Troponin senses Ca2+ to regulate contraction in striated muscle. Structures of skeletal muscle troponin composed of TnC (the sensor), TnI (the regulator), and TnT (the link to the muscle thin filament) have been determined. The structure of troponin in the Ca(2+)-activated state features a nearly twofold symmetrical assembly of TnI and TnT subunits penetrated asymmetrically by the dumbbell-shaped TnC subunit. Ca ions are thought to regulate contraction by controlling the presentation to and withdrawal of the TnI inhibitory segment from the thin filament. Here, we show that the rigid central helix of the sensor binds the inhibitory segment of TnI in the Ca(2+)-activated state. Comparison of crystal structures of troponin in the Ca(2+)-activated state at 3.0 angstroms resolution and in the Ca(2+)-free state at 7.0 angstroms resolution shows that the long framework helices of TnI and TnT, presumed to be a Ca(2+)-independent structural domain of troponin are unchanged. Loss of Ca ions causes the rigid central helix of the sensor to collapse and to release the inhibitory segment of TnI. The inhibitory segment of TnI changes conformation from an extended loop in the presence of Ca2+ to a short alpha-helix in its absence. We also show that Anapoe, a detergent molecule, increases the contractile force of muscle fibers and binds specifically, together with the TnI switch helix, in a hydrophobic pocket of TnC upon activation by Ca ions.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.