Protein 4.1R core domain structure and insights into regulation of cytoskeletal organization
Protein 4.1R core domain structure and insights into regulation of cytoskeletal organization
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DOI：
10.1038/82819
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发表时间：
2000-10
期刊：
影响因子：
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通讯作者：
B. Han;W. Nunomura;Y. Takakuwa;N. Mohandas;B. Jap
中科院分区：
文献类型：
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作者：
B. Han;W. Nunomura;Y. Takakuwa;N. Mohandas;B. Jap
细胞骨架蛋白4.1 R的核心结构域（N-末端30 kDa结构域）的晶体结构已被确定，并显示出三叶草状的架构。三叶草的每一个叶都含有一个带3、血型糖蛋白C/D或p55的特异性结合位点。在分子的中心区域，靠近三个叶连接的地方是两个独立的钙调蛋白（CaM）结合区域。其中一个主要由α-螺旋组成，对Ca 2+不敏感;另一个呈伸展结构，Ca 2+的存在显著增强了其与CaM的结合，导致蛋白4.1R与其靶蛋白的结合减弱。这种新的结构，其中三个叶与三个膜相关蛋白结合，钙调素结合位点的位置提供了深入了解蛋白4.1 R核心结构域如何与膜蛋白相互作用，并动态调节细胞形状，响应细胞内Ca 2+水平的变化。
The crystal structure of the core domain (N-terminal 30 kDa domain) of cytoskeletal protein 4.1 R has been determined and shows a cloverleaf-like architecture. Each lobe of the cloverleaf contains a specific binding site for either band 3, glycophorin C/D or p55. At a central region of the molecule near where the three lobes are joined are two separate calmodulin (CaM) binding regions. One of these is composed primarily of an α-helix and is Ca 2+ insensitive; the other takes the form of an extended structure and its binding with CaM is dramatically enhanced by the presence of Ca 2+, resulting in the weakening of protein 4.1 R binding to its target proteins. This novel architecture, in which the three lobes bind with three membrane associated proteins, and the location of calmodulin binding sites provide insight into how the protein 4.1 R core domain interacts with membrane proteins and dynamically regulates cell shape in response to changes in intracellular Ca 2+ levels.