PulseExploreJournal ClubDebatesTrendingResearchersJournals
Instagram
HomeExploreJournal ClubTrending
Synapse
⌘+K
Synapse
November 1, 1994Journal of Biological Chemistry234 citationsOpen Access

Binding of a new Ca2+ sensitizer, levosimendan, to recombinant human cardiac troponin C. A molecular modelling, fluorescence probe, and proton nuclear magnetic resonance study.

View Full Paper
PPPiero PolleselloMOMartti OvaskaJKJuha Kaivola

Key Result

Levosimendan binds to the hydrophobic pocket of the NH2-terminal domain of human cardiac troponin C, modulating the calcium-induced conformational change.

Key Points

  • This study aims to elucidate the binding mechanism of levosimendan to cardiac troponin C and its impact on calcium sensitivity.
  • Conducted fluorescence studies on recombinant human cardiac troponin C and site-directed mutants.
  • Performed NMR studies on the NH2-terminal fragment of cardiac troponin C.
  • Built an optimized model of the drug-protein complex to analyze binding sites.
  • Levosimendan modulated calcium-induced conformational changes in cardiac troponin C.
  • Binding was associated with Asp-88's role in the NH2-terminal domain, showing spatial proximity to key residues.
  • An optimized model indicated levosimendan binds at the hydrophobic pocket of the protein.

Structured PICO

P
Population
Recombinant human cardiac troponin C (cTnC) and a site-directed mutant
I
Intervention
Levosimendan
O
Outcome
Binding characteristics and conformational changes of cTnCsurrogate

Levosimendan acts as a calcium sensitizer by binding to the hydrophobic pocket of the NH2-terminal domain of cardiac troponin C.

Abstract

The binding of a new calcium sensitizer, levosimendan, to human cardiac troponin C (cTnC) is described. Fluorescence studies done on dansylated recombinant human cTnC and a site-directed mutant showed that levosimendan modulated the calcium-induced conformational change in cTnC, and revealed the role of Asp-88 in the binding of the drug to the NH2-terminal domain of cTnC. Furthermore, NMR studies performed on the NH2-terminal fragment of cTnC showed a spatial proximity between levosimendan and Met81, Met85, and Phe77 in the drug-protein complex. These data were used to build an optimized model of the drug-protein complex, in which levosimendan binds cTnC at the hydrophobic pocket of the NH2-terminal domain. The role of the binding of levosimendan to cTnC in the pharmacological action of this drug in vivo is discussed.

Ask AI
Helpful
Bookmark
Share
View Full Paper

Cite This Study

Pollesello et al. (1994) studied this question. Levosimendan was evaluated on Binding of levosimendan to human cardiac troponin C. Levosimendan binds to the hydrophobic pocket of the NH2-terminal domain of human cardiac troponin C, modulating the calcium-induced conformational change.

synapsesocial.com/papers/6a07e28f416812afca06e5bahttps://doi.org/10.1016/s0021-9258(19)61945-9
Ask AI
Helpful
Bookmark
Share
View Full Paper