High-resolution model of the microtubule
High-resolution model of the microtubule
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DOI：
10.1016/s0092-8674(00)80961-7
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发表时间：
1999-01-08
期刊：
影响因子：
64.5
通讯作者：
Downing, KH
中科院分区：
文献类型：
--
作者：
Nogales, E;Whittaker, M;Downing, KH
通过将微管蛋白的晶体结构对接到微管的20埃图中，获得了微管的高分辨率模型。良好的拟合度表明了两种聚合物中微管蛋白构象的相似性，并确定了微管中微管蛋白结构的取向。长的C末端螺旋形成原细丝外部的顶端，而长环则定义微管腔。β-微管蛋白中可交换的核苷酸暴露在微管的正端，而建议的α-微管蛋白中的催化残基暴露在负端。单体之间广泛的纵向界面具有极性和疏水性成分。在侧向接触处，核苷酸敏感的螺旋与有助于紫杉醇在β-微管蛋白中的结合位置的环相互作用。
A high-resolution model of the microtubule has been obtained by docking the crystal structure of tubulin into a 20 Angstrom map of the microtubule. The excellent fit indicates the similarity of the tubulin conformation in both polymers and defines the orientation of the tubulin structure within the microtubule. Long C-terminal helices form the crest on the outside of the protofilament, while long loops define the microtubule lumen. The exchangeable nucleotide in beta-tubulin is exposed at the plus end of the microtubule, while the proposed catalytic residue in alpha-tubulin is exposed at the minus end. Extensive longitudinal interfaces between monomers have polar and hydrophobic components. At the lateral contacts, a nucleotide-sensitive helix interacts with a loop that contributes to the binding site of taxol in beta-tubulin.