TARGET ENZYME RECOGNITION BY CALMODULIN - 2.4-ANGSTROM STRUCTURE OF A CALMODULIN-PEPTIDE COMPLEX
TARGET ENZYME RECOGNITION BY CALMODULIN - 2.4-ANGSTROM STRUCTURE OF A CALMODULIN-PEPTIDE COMPLEX
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DOI：
10.1126/science.1519061
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发表时间：
1992-08-28
期刊：
影响因子：
56.9
通讯作者：
QUIOCHO, FA
中科院分区：
文献类型：
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作者：
MEADOR, WE;MEANS, AR;QUIOCHO, FA
钙结合的钙调素（Ca ~（2+）-CaM）结合到鸡平滑肌肌球蛋白轻链激酶的CaM结合区的肽类似物的晶体结构已被确定和细化到2.4埃（埃）的分辨率。结构紧凑，具有椭圆体的形状（轴比约为2：1）。结合的钙调素形成了一个隧道对角线的长轴，吞噬螺旋肽，与钙调素的疏水区融合成一个单一的区域，紧密覆盖的疏水侧的肽。有一个非常高的伪二重对称性密切相关的领域之间。天然CaM的中心螺旋解绕并扩展成残基73和77之间的弯曲。2018年10月15日，《中国日报》（
The crystal structure of calcium-bound calmodulin (Ca2+-CaM) bound to a peptide analog of the CaM-binding region of chicken smooth muscle myosin light chain kinase has been determined and refined to a resolution of 2.4 angstroms (angstrom). The structure is compact and has the shape of an ellipsoid (axial ratio approximately 2:1). The bound CaM forms a tunnel diagonal to its long axis that engulfs the helical peptide, with the hydrophobic regions of CaM melded into a single area that closely covers the hydrophobic side of the peptide. There is a remarkably high pseudo-twofold symmetry between the closely associated domains. The central helix of the native CaM is unwound and expanded into a bend between residues 73 and 77. About 185 contacts (