Molecular structure of troponin C from chicken skeletal muscle at 3-angstrom resolution.
Molecular structure of troponin C from chicken skeletal muscle at 3-angstrom resolution.
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鸡骨骼肌肌钙蛋白 C 的分子结构，分辨率为 3 埃。
DOI：
10.1126/science.3969570
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发表时间：
1985
期刊：
影响因子：
--
通讯作者：
Wang,BC
中科院分区：
文献类型：
--
作者：
Sundaralingam,M;Bergstrom,R;Strasburg,G;Rao,ST;Roychowdhury,P;Greaser,M;Wang,BC
鸡骨骼肌肌钙蛋白C（TnC）是肌钙蛋白复合物的Ca 2+结合亚基，其X射线结构显示，该蛋白质长约70埃，具有不寻常的哑铃形状。羧基和氨基结构域由一个约9圈的长α螺旋分开。只有两个高亲和力的Ca 2 +-Mg 2+网站的COOH-域被金属离子占据，导致COOH-和NH 2-域之间的构象差异。这些差异可能在由TnC触发肌肉收缩中是重要的。此外，TnC的结构与理解其他钙调节蛋白的功能有关，特别是钙调蛋白，因为其氨基酸序列具有很强的相似性。
The x-ray structure of chicken skeletal muscle troponin C (TnC), the Ca2+-binding subunit of the troponin complex, shows that the protein is about 70 angstroms long with an unusual dumbbell shape. The carboxyl and amino domains are separated by a single long α helix of about nine turns. Only the two high-affinity Ca2+-Mg2+sites of the COOH-domain are occupied by metal ions resulting in conformational differences between the COOH- and NH2-domains. These differences are probably important in the triggering of muscle contraction by TnC. Also the structure of TnC is relevant in understanding the function of other calcium-regulated proteins, in particular that of calmodulin because of its strong similarity in amino acid sequence.