The interaction of the bisphosphorylated N-terminal arm of cardiac troponin I-A 31P-NMR study

被引：9
|
作者：
Schmidtmann, A [1 ]
Lohmann, K [1 ]
Jaquet, K [1 ]
机构：
[1] Ruhr Univ Bochum, Fak Med, Biochem Supramolek Syst Abt, D-44780 Bochum, Germany
来源：
FEBS LETTERS | 2002年 / 513卷 / 2-3期
关键词：
P-31-nuclear magnetic resonance; cardiac troponin; cardiac troponin I; cardiac troponin C; cardiac troponin T;
D O I：
10.1016/S0014-5793(02)02340-2
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Cardiac troponin I, the inhibitory subunit of the heterotrimeric cardiac troponin (cTn) complex is phosphorylated by protein kinase A at two serine residues located in its heart-specific NI-terminal extension. This flexible arm interacts at different sites within cTn dependent on its phosphorylation degree. BisphosphoryIation is known to induce conformational changes within cTnI which finally lead to a reduction of the calcium affinity of cTnC. However, as we show here, the bisphosphorylated cTnI arm does not interact with cTnC, but with cTnT and/or cTnI. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
引用
收藏
页码：289 / 293
页数：5
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