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-Structure paper
タイトル | The Ndc80 kinetochore complex forms oligomeric arrays along microtubules. |
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ジャーナル・号・ページ | Nature, Vol. 467, Issue 7317, Page 805-810, Year 2010 |
掲載日 | 2010年10月14日 |
著者 | Gregory M Alushin / Vincent H Ramey / Sebastiano Pasqualato / David A Ball / Nikolaus Grigorieff / Andrea Musacchio / Eva Nogales / |
PubMed 要旨 | The Ndc80 complex is a key site of regulated kinetochore-microtubule attachment (a process required for cell division), but the molecular mechanism underlying its function remains unknown. Here we ...The Ndc80 complex is a key site of regulated kinetochore-microtubule attachment (a process required for cell division), but the molecular mechanism underlying its function remains unknown. Here we present a subnanometre-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 the Ndc80 complex binds the microtubule with a tubulin monomer repeat, recognizing α- and β-tubulin at both intra- and inter-tubulin dimer interfaces in a manner that is sensitive to tubulin conformation. Furthermore, Ndc80 complexes self-associate along protofilaments through interactions mediated by the amino-terminal tail of the NDC80 protein, which is the site of phospho-regulation by Aurora B kinase. The complex's mode of interaction with the microtubule and its oligomerization suggest a mechanism by which Aurora B could regulate the stability of load-bearing kinetochore-microtubule attachments. |
リンク | Nature / PubMed:20944740 / PubMed Central |
手法 | EM (らせん対称) |
解像度 | 8.6 Å |
構造データ | |
化合物 | ChemComp-ZN: ChemComp-MG: ChemComp-GTP: ChemComp-GDP: ChemComp-TA1: |
由来 |
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キーワード | CELL CYCLE (細胞周期) / Ndc80 / HEC1 / NUF2 / tubulin (チューブリン) / kinetochore (動原体) / mitosis (有糸分裂) / calponin homology domain / microtubule (微小管) |