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Article

Folding and function of the troponin tail domain. Effects of cardiomyopathic troponin T mutations.

The Journal of biological chemistry - 3 Jan 2003

Hinkle Ashley, Tobacman Larry S

Abstract excerpt

Troponin contains a globular Ca(2+)-binding domain and an elongated tail domain composed of the N terminus of subunit troponin T (TnT). The tail domain anchors troponin to tropomyosin and actin, modulates myosin function, and is a site of cardiomyopathy-inducing mutations. Critical interactions between tropomyosin and troponin are proposed to depend on tail domain residues 112-136, which are highly conserved...

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Identifiers

PMID: 12409295
DOI: 10.1074/jbc.M209194200

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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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