The Ndc80 kinetochore complex forms oligomeric arrays along microtubules.
The Ndc80 kinetochore complex forms oligomeric arrays along microtubules.
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Ndc 80复合物是一个关键的网站，调节kinetochore-microtubule附件，但其功能的分子机制仍然未知。在这里，我们提出了一个亚纳米分辨率冷冻电子显微镜重建的人类Ndc 80复合物结合微管，足以精确对接的组成蛋白质的晶体结构。我们发现，Ndc 80结合微管与微管蛋白单体重复，识别α-和β-微管蛋白在内部和内部二聚体接口的方式是敏感的微管蛋白构象。此外，Ndc 80复合物通过Ndc 80蛋白的氨基末端尾（极光B激酶磷酸化调节的位点）介导的相互作用沿着沿着原丝自缔合。Ndc 80与微管的相互作用模式及其寡聚化表明Aurora B可以调节负载Ndc 80-微管附着的稳定性的机制。
The Ndc80 complex is a key site of regulated kinetochore-microtubule attachment, but the molecular mechanism underlying its function remains unknown. Here we present a subnanometer resolution cryo-electron microscopy reconstruction of the human Ndc80 complex bound to microtubules, sufficient for precise docking of crystal structures of the component proteins. We find that Ndc80 binds the microtubule with a tubulin monomer repeat, recognizing α- and β-tubulin at both intra- and inter-dimer interfaces in a manner that is sensitive to tubulin conformation. Furthermore, Ndc80 complexes self-associate along protofilaments via interactions mediated by the amino-terminal tail of the Ndc80 protein, the site of phospho-regulation by the Aurora B kinase. Ndc80's mode of interaction with the microtubule and its oligomerization suggest a mechanism by which Aurora B could regulate the stability of load-bearing Ndc80-microtubule attachments.
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DOI：
10.1016/j.cub.2008.08.012
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