Inhibition of mutant troponin C activity by an intra-domain disulphide bond.

doi:10.1038/345132a0

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Article

Inhibition of mutant troponin C activity by an intra-domain disulphide bond.

Nature - 10 May 1990

Grabarek Z, Tan R Y, Wang J, Tao T, Gergely J

Abstract excerpt

Triggering of contraction in striated muscles involves a conformational transition in the N-terminal domain of troponin C, the calcium-binding component of thin filaments. We have designed a mutant troponin C in which the key conformational transition and the calcium-regulatory activity are reversibly blocked by the formation of a disulphide bridge. Our results may be applicable to other proteins of the same...

Topics

Animals
Aziridines
Binding Sites
Calcium
Crystallization
Dansyl Compounds
Disulfides
Dithiothreitol
Edetic Acid
Fluorescent Dyes
Muscle Contraction
Mutation

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Protein Conformation

Rabbits

Spectrometry, Fluorescence

Structure-Activity Relationship

Troponin

Troponin C

Source

Open in PubMed

Identifiers

PMID: 2110625
DOI: 10.1038/345132a0

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-2110625-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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