A self-consistent field analysis of the neurofilament brush with amino-acid resolution.
A self-consistent field analysis of the neurofilament brush with amino-acid resolution.
复制标题
对神经丝刷进行氨基酸分辨率的自洽现场分析。
DOI：
10.1529/biophysj.106.095323
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发表时间：
2007
影响因子：
3.4
通讯作者：
Frans A. M. Leermakers
中科院分区：
文献类型：
--
作者：
E. Zhulina;Frans A. M. Leermakers
利用Scheutjens和Fleer的数值模型，我们在自一致场水平上研究了由NF-H、NF-M和NF-L蛋白的投射域形成的神经丝刷的平衡结构。虽然实际的氨基酸序列在投射区域是粗粒度的，但氨基酸残基的不同（实际）溶解度及其内在电荷在NF蛋白臂内的特定分布被明确地考虑在内。我们收集了强有力的证据，表明静电相互作用是控制NF电刷结构的主导力量。H、M、L尾存在显著的空间分离。在去磷酸化的NF中，我们分别发现H和M投射域的受限构象和花状构象。我们证明了NF蛋白中KSP重复序列的电离触发了H尾部的构象转变，导致其末端（KEP）结构域被驱逐到NF刷的外围。我们认为，轴突中NF蛋白的磷酸化既可以增加神经丝间的距离，又可以稳定神经丝之间的交叉桥。
Using the numerical model of Scheutjens and Fleer we investigated, on a self-consistent field level, the equilibrium structure of the neurofilament brush formed by the projection domains of NF-H, NF-M, and NF-L proteins. Although the actual amino-acid sequences in the projection domains are coarse-grained, the different (realistic) solubilities of amino-acid residues and the specific distribution of its intrinsic charges inside the arms of the NF proteins are taken explicitly into account. We collect strong evidence that the electrostatic interactions are a dominant force that controls the NF brush structure. There exists a remarkable spatial separation of the H, M, and L tails. In a dephosphorylated NF we found confined and flowerlike conformations for the H and M projection domains, respectively. We demonstrate that the ionization of KSP repeats in NF proteins triggers a conformational transition in the H tail that leads to the expulsion of its terminal (KEP) domain to the periphery of the NF brush. We argue that the phosphorylation of the NF proteins in axons can both increase the interfilament distance and stabilize cross bridges between neurofilaments.
DOI：
10.1073/pnas.84.10.3472
发表时间：
1987-05-01
影响因子：
11.1
作者：
HOFFMAN, PN;CLEVELAND, DW;PRICE, DL
通讯作者：
PRICE, DL
影响因子：
3.4
作者：
Kumar, S;Yin, XH;Paulaitis, ME
通讯作者：
Paulaitis, ME