MODULATION OF CALMODULIN PLASTICITY IN MOLECULAR RECOGNITION ON THE BASIS OF X-RAY STRUCTURES
MODULATION OF CALMODULIN PLASTICITY IN MOLECULAR RECOGNITION ON THE BASIS OF X-RAY STRUCTURES
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DOI：
10.1126/science.8259515
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发表时间：
1993-12-10
期刊：
影响因子：
56.9
通讯作者：
QUIOCHO, FA
中科院分区：
文献类型：
--
作者：
MEADOR, WE;MEANS, AR;QUIOCHO, FA
钙调素是主要的钙依赖性信号转导和调节各种基本细胞功能。结合到对应于脑钙调蛋白依赖性蛋白激酶II α的钙调蛋白结合结构域的肽的钙-钙调蛋白的结构被确定为2埃分辨率。与其他两种钙-钙调蛋白结构的比较揭示了中央螺旋如何展开，以便在识别不同的靶酶时最佳地定位两个结构域，并澄清了钙在维持转录主管结构域结构中的作用。
Calmodulin is the primary calcium-dependent signal transducer and regulator of a wide variety of essential cellular functions. The structure of calcium-calmodulin bound to the peptide corresponding to the calmodulin-binding domain of brain calmodulin-dependent protein kinase IIalpha was determined to 2 angstrom resolution. A comparison to two other calcium-calmodulin structures reveals how the central helix unwinds in order to position the two domains optimally in the recognition of different target enzymes and clarifies the role of calcium in maintaining recognition-competent domain structures.