Cardiac troponin I inhibitory peptide: location of interaction sites on troponin C
Cardiac troponin I inhibitory peptide: location of interaction sites on troponin C
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DOI：
10.1016/s0014-5793(00)01271-0
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发表时间：
2000-03-10
期刊：
影响因子：
3.5
通讯作者：
Rosevear, PR
中科院分区：
文献类型：
--
作者：
Abbott, MB;Dvoretsky, A;Rosevear, PR
心肌肌钙蛋白I（129-149）在两个不同位点与钙饱和心肌肌钙蛋白C/肌钙蛋白I（1-80）复合物结合。发现第一当量肌钙蛋白I（129-149）的结合主要影响调节结构域中的酰胺质子化学位移，而第二当量干扰D/E接头区域内的酰胺质子化学位移。氮-15的横向弛豫速率表明，结合的第一个当量的抑制肽的调节结构域降低了构象交换失效的钙结合位点I和，另外的第二个当量的抑制肽的D/E接头区域的灵活性降低。通过这些方法未检测到抑制肽与心肌肌钙蛋白C的C结构域之间的相互作用，表明抑制肽不能从C结构域置换cTnI（1-80）。(C)2000年欧洲生物化学学会联合会。
Cardiac troponin I(129-149) binds to the calcium saturated cardiac troponin C/troponin I(1-80) complex at two distinct sites. Binding of the first equivalent of troponin I(129-149) was found to primarily affect amide proton chemical shifts in the regulatory domain, while the second equivalent perturbed amide proton chemical shifts within the D/E linker region. Nitrogen-15 transverse relaxation rates showed that binding the first equivalent of inhibitory peptide to the regulatory domain decreased conformational exchange in defunct calcium binding site I and that addition of the second equivalent of inhibitory peptide decreased flexibility in the D/E linker region. No interactions between the inhibitory peptide and the C-domain of cardiac troponin C were detected by these methods demonstrating that the inhibitory peptide cannot displace cTnI(1-80) from the C-domain. (C) 2000 Federation of European Biochemical Societies.