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Article

The muscle-relaxing C-terminal peptide from troponin I populates a nascent helix, facilitating binding to tropomyosin with a potent therapeutic effect.

The Journal of biological chemistry - 1 Jan 2000

Hornos Felipe, Feng Han-Zhong, Rizzuti Bruno, Palomino-Schätzlein Martina, Wieczorek David, Neira José L, Jin J-P

Abstract excerpt

The conserved C-terminal end segment of troponin I (TnI) plays a critical role in regulating muscle relaxation. This function is retained in the isolated C-terminal 27 amino acid peptide (residues 184-210) of human cardiac TnI (HcTnI-C27): When added to skinned muscle fibers, HcTnI-C27 reduces the Ca2+-sensitivity of activated myofibrils and facilitates relaxation without decreasing the maximum force production....

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Share to Cardiomyopathy, Hypertrophic
Share to Molecular Docking Simulation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Share to Muscle Fibers, Skeletal

Share to Myofibrils

Share to Protein Conformation, alpha-Helical

Share to Protein Interaction Domains and Motifs

Share to Tropomyosin

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Source

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Identifiers

PMID: 33814345
DOI: 10.1074/jbc.RA120.016012
PMCID: PMC7948816

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

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