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首页> 外文期刊>Nature >Structural basis for activation of the titin kinase domain during myofibrillogenesis (see comments) (published erratum appears in Nature 1999 Feb 25;397(6712):719)
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Structural basis for activation of the titin kinase domain during myofibrillogenesis (see comments) (published erratum appears in Nature 1999 Feb 25;397(6712):719)

机译：在肌原纤维形成过程中激活titin激酶结构域的结构基础（见评论）（发表的勘误出现在Nature 1999 Feb 25; 397（6712）：719）

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摘要

The giant muscle protein titin (connectin) is essential in the temporal and spatial control of the assembly of the highly ordered sarcomeres (contractile units) of striated muscle. Here we present the crystal structure of titin's only catalytic domain, an autoregulated serine kinase (titin kinase). The structure shows how the active site is inhibited by a tyrosine of the kinase domain. We describe a dual mechanism of activation of titin kinase that consists of phosphorylation of this tyrosine and binding of calcium/calmodulin to the regulatory tail. The serine kinase domain of titin is the first known non-arginine-aspartate kinase to be activated by phosphorylation. The phosphorylated tyrosine is not located in the activation segment, as in other kinases, but in the P + 1 loop, indicating that this tyrosine is a binding partner of the titin kinase substrate. Titin kinase phosphorylates the muscle protein telethonin in early differentiating myocytes, indicating that this kinase may act in myofibrillogenesis.
机译：巨大的肌肉蛋白滴定蛋白（connectin）在横纹肌高度有序的肉瘤（收缩单位）的组装的时间和空间控制中至关重要。在这里，我们介绍了titin唯一的催化结构域，一种自动调节的丝氨酸激酶（titin激酶）的晶体结构。该结构显示了活性位点如何被激酶域的酪氨酸抑制。我们描述了由该酪氨酸的磷酸化和钙/钙调蛋白与调节性尾巴的结合组成的titin激酶活化的双重机制。丝氨酸的丝氨酸激酶结构域是第一个已知的通过磷酸化激活的非精氨酸-天冬氨酸激酶。磷酸化的酪氨酸不像其他激酶那样位于活化段中，而是位于P +1环中，表明该酪氨酸是titin激酶底物的结合伴侣。 Titin激酶使早期分化的心肌细胞中的肌肉蛋白Telethonin磷酸化，表明该激酶可能在肌原纤维形成中起作用。

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