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-Structure paper
Title | Multimodal microtubule binding by the Ndc80 kinetochore complex. |
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Journal, issue, pages | Nat Struct Mol Biol, Vol. 19, Issue 11, Page 1161-1167, Year 2012 |
Publish date | Oct 21, 2012 |
Authors | Gregory M Alushin / Vivek Musinipally / Daniel Matson / John Tooley / P Todd Stukenberg / Eva Nogales / |
PubMed Abstract | The Ndc80 complex is a key site of kinetochore-microtubule attachment during cell division. The human complex engages microtubules with a globular 'head' formed by tandem calponin-homology domains ...The Ndc80 complex is a key site of kinetochore-microtubule attachment during cell division. The human complex engages microtubules with a globular 'head' formed by tandem calponin-homology domains and an 80-amino-acid unstructured 'tail' that contains sites of phosphoregulation by the Aurora B kinase. Using biochemical, cell biological and electron microscopy analyses, we dissected the roles of the tail in binding of microtubules and mediation of cooperative interactions between Ndc80 complexes. Two segments of the tail that contain Aurora B phosphorylation sites become ordered at interfaces; one with tubulin and the second with an adjacent Ndc80 head on the microtubule surface, forming interactions that are disrupted by phosphorylation. We propose a model in which Ndc80's interaction with either growing or shrinking microtubule ends can be tuned by the phosphorylation state of its tail. |
External links | Nat Struct Mol Biol / PubMed:23085714 / PubMed Central |
Methods | EM (helical sym.) |
Resolution | 7.9 - 13.0 Å |
Structure data | EMDB-5489: EMDB-5490: EMDB-5491: EMDB-5492: EMDB-5493: |
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