July 1, 2000Journal of Biological ChemistryOpen Access

Regulatory Domain Conformational Exchange and Linker Region Flexibility in Cardiac Troponin C Bound to Cardiac Troponin I

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Population

Cardiac troponin C and cardiac troponin I complexes (in vitro protein models)

Comparison

Binding to intact cardiac troponin I, addition… vs Isolated N-domain of cardiac troponin I or…

Design

Preclinical

Authors

MAM.Bret AbbottUniversity of Alabama at Birmingham VGVadim GaponenkoUniversity of Illinois Chicago EAEkram AbusamhadnehLos Alamos National Laboratory

Discussion

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Implication

Highlights troponin phosphorylation effects in vitro; leaves open in vivo cardiac function or therapeutic relevance.

Structured PICO

Population

Cardiac troponin C and cardiac troponin I complexes (in vitro protein models)

Intervention

Binding to intact cardiac troponin I, addition of 2 M urea, and binding to various troponin I fragments (1-211, 33-211, 1-80, bisphosphorylated 1-80)

Comparator

Isolated N-domain of cardiac troponin I or unphosphorylated fragments

Outcome

Conformational changes in the regulatory domain and linker flexibility of cardiac troponin Csurrogate

The cardiac specific N terminus of troponin I can modulate troponin C function by altering the conformational equilibrium of its regulatory domain, an effect that is reversed by phosphorylation.

Cite This Study

Abbott et al. (2000) studied this question.

synapsesocial.com/papers/6a83d8e7a3cef8348e9975d1 https://doi.org/10.1074/jbc.m909252199

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Regulatory Domain Conformational Exchange and Linker Region Flexibility in Cardiac Troponin C Bound to Cardiac Troponin I

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Regulatory Domain Conformational Exchange and Linker Region Flexibility in Cardiac Troponin C Bound to Cardiac Troponin I

Discussion

Member takes

Implication

Structured PICO

Cite This Study

Also Consider

Also Consider