Discover Community Create You

Loading publication...

Noodle always counts identifier-free feature events for service operation. With your permission, Google Analytics can also estimate audience and engagement. Search text, publication identifiers, cookies, IP addresses and browser fingerprints are never included in Noodle's first-party event counters.

Privacy details

Article

Probing the calcium-induced conformational transition of troponin C with site-directed mutants.

Nature - 10 May 1990

Fujimori K, Sorenson M, Herzberg O, Moult J, Reinach F C

Abstract excerpt

The contraction of skeletal muscle is regulated by calcium binding to troponin C (TnC). TnC consists of two spatially independent domains, each of which contains two metal ion binding sites. Calcium binding to the regulatory sites of the N-terminal domain triggers muscle contraction by a series of conformational changes. Site-directed mutagenesis offers a means of elucidating the links in this signal path between...

Read the complete abstract on PubMed

Topics

Share this publication in a Topic to start or enrich a Post.

Share to Binding Sites
Share to Escherichia coli
Share to Hydrogen-Ion Concentration

Methodology Data sources Editorial policy Privacy Delete account & data About Contact Helena Bioinformatics

Share to Mutation

Share to Protein Conformation

Share to Recombinant Proteins

Share to Signal Transduction

Share to Structure-Activity Relationship

Source

Identifiers

PMID: 2186281
DOI: 10.1038/345182a0

Provenance

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

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

Semantic proximity does not establish scientific evidence. Graph snapshot: 2026-09-29.

Research trail→

Click a neighbor to travelStep 1 · 12 closest

Probing the calcium-induced conformational transition of troponin C with site-directed mutants.PMID 2186281Read ↗

Troponin-C mutants with increased calcium affinity.Semantic proximity Read ↗

Designing calcium-sensitizing mutations in the regulatory domain of cardiac troponin C.Semantic proximity Read ↗

Inhibition of mutant troponin C activity by an intra-domain disulphide bond.Semantic proximity Read ↗

Calcium affinity of regulatory sites in skeletal troponin-C is attenuated by N-cap mutations of helix C.Semantic proximity Read ↗

Mutations in the N- and D-helices of the N-domain of troponin C affect the C-domain and regulatory function.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 ↗

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 ↗

Structure of the troponin complex. Implications of photocross-linking of troponin I to troponin C thiol mutants.Semantic proximity Read ↗

Intramolecular interactions in the N-domain of cardiac troponin C are important determinants of calcium sensitivity of force development.Semantic proximity Read ↗

Mutation of the high affinity calcium binding sites in cardiac troponin C.Semantic proximity Read ↗

Structural and functional consequences of cardiac troponin C L57Q and I61Q Ca(2+)-desensitizing variants.Semantic proximity Read ↗

Changes in the dynamics of the cardiac troponin C molecule explain the effects of Ca2+-sensitizing mutations.Semantic proximity Read ↗

⌁Select a neighboring publication to make it the new centre.