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Article

Ca(2+) induces an extended conformation of the inhibitory region of troponin I in cardiac muscle troponin.

Journal of molecular biology - 16 Nov 2001

Dong W J, Xing J, Robinson J M, Cheung H C

Abstract excerpt

The inhibitory region of troponin I (TnI) plays a central regulatory role in the contraction and relaxation cycle of skeletal and cardiac muscle through its Ca(2+)-dependent interaction with actin. Detailed structural information on the interface between TnC and this region of TnI has been long in dispute. We have used fluorescence resonance energy transfer (FRET) to investigate the global conformation of the...

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Identifiers

PMID: 11724531
DOI: 10.1006/jmbi.2001.5118

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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Ca(2+) induces an extended conformation of the inhibitory region of troponin I in cardiac muscle troponin.PMID 11724531Read ↗

Structural and functional studies on Troponin I and Troponin C interactions.Semantic proximity Read ↗

Conformation of the regulatory domain of cardiac muscle troponin C in its complex with cardiac troponin I.Semantic proximity Read ↗

Ca2+-dependent interaction of the inhibitory region of troponin I with acidic residues in the N-terminal domain of troponin C.Semantic proximity Read ↗

Dynamics of the C-terminal region of TnI in the troponin complex in solution.Semantic proximity Read ↗

Proximity relationships between residue 117 of rabbit skeletal troponin-I and residues in troponin-C and actin.Semantic proximity Read ↗

Structural kinetics of cardiac troponin C mutants linked to familial hypertrophic and dilated cardiomyopathy in troponin complexes.Semantic proximity Read ↗

Structure of the inhibitory region of troponin by site directed spin labeling electron paramagnetic resonance.Semantic proximity Read ↗

Phosphorylation-induced distance change in a cardiac muscle troponin I mutant.Semantic proximity Read ↗

Mutations of hydrophobic residues in the N-terminal domain of troponin C affect calcium binding and exchange with the troponin C-troponin I96-148 complex and muscle force production.Semantic proximity Read ↗

Evidence for two-site binding of troponin I inhibitory peptides to the N and C domains of troponin C.Semantic proximity Read ↗

Switch action of troponin on muscle thin filament as revealed by spin labeling and pulsed EPR.Semantic proximity Read ↗

The C terminus of cardiac troponin I stabilizes the Ca2+-activated state of tropomyosin on actin filaments.Semantic proximity Read ↗

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