Interaction between troponin I and troponin C

The spatial proximity on the surface of troponin C for sites specific for peptides CN4 (res. 96–116) and CN5 (res. 1–21) of troponin I has been demonstrated by proton magnetic resonance spectroscopy. The broadened signals from each peptide are at similar radial distances from the paramagnetic spin l...

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Bibliographic Details
Published inFEBS letters Vol. 150; no. 1; pp. 54 - 58
Main Authors Dalgarno, D.C., Grand, R.J.A., Levine, B.A., Moir, A.J.G., Scott, G.M.M., Perry, S.V.
Format Journal Article
LanguageEnglish
Published 13.12.1982
Subjects
Calcium-binding
Muscle
Proton magnetic resonance spectroscopy
Spin labelling
Troponin C
Troponin I
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Summary:The spatial proximity on the surface of troponin C for sites specific for peptides CN4 (res. 96–116) and CN5 (res. 1–21) of troponin I has been demonstrated by proton magnetic resonance spectroscopy. The broadened signals from each peptide are at similar radial distances from the paramagnetic spin label bound to Cys 98 of troponin C. A U‐shaped disposition of peptide CN5 about Cys 98 is indicated, the interaction being modulated by calcium binding to the low affinity Ca2+ domains of troponin C. Paramagnetic broadening of signals from peptide CN4 was observed on addition of peptide TR2 (res. 88–159) from spin‐labelled troponin C, a region that contains the higher affinity Ca2+ domains.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(82)81303-3