4C9Y
Structural Basis for the microtubule binding of the human kinetochore Ska complex
Summary for 4C9Y
Entry DOI | 10.2210/pdb4c9y/pdb |
Related | 4CA0 |
Descriptor | SPINDLE AND KINETOCHORE-ASSOCIATED PROTEIN 1 (2 entities in total) |
Functional Keywords | cell cycle, cell divison, kinetochore-microtubule attachment, winged-helix domain |
Biological source | HOMO SAPIENS (HUMAN) |
Cellular location | Cytoplasm, cytoskeleton, spindle: Q96BD8 |
Total number of polymer chains | 2 |
Total formula weight | 29307.20 |
Authors | Abad, M.,Medina, B.,Santamaria, A.,Zou, J.,Plasberg-Hill, C.,Madhumalar, A.,Jayachandran, U.,Redli, P.M.,Rappsilber, J.,Nigg, E.A.,Jeyaprakash, A.A. (deposition date: 2013-10-04, release date: 2014-01-22) |
Primary citation | Abad, M.A.,Medina, B.,Santamaria, A.,Zou, J.,Plasberg-Hill, C.,Madhumalar, A.,Jayachandran, U.,Redli, P.M.,Rappsilber, J.,Nigg, E.A.,Jeyaprakash, A.A. Structural Basis for Microtubule Recognition by the Human Kinetochore Ska Complex. Nat.Commun., 5:2964-, 2014 Cited by PubMed Abstract: The ability of kinetochores (KTs) to maintain stable attachments to dynamic microtubule structures ('straight' during microtubule polymerization and 'curved' during microtubule depolymerization) is an essential requirement for accurate chromosome segregation. Here we show that the kinetochore-associated Ska complex interacts with tubulin monomers via the carboxy-terminal winged-helix domain of Ska1, providing the structural basis for the ability to bind both straight and curved microtubule structures. This contrasts with the Ndc80 complex, which binds straight microtubules by recognizing the dimeric interface of tubulin. The Ska1 microtubule-binding domain interacts with tubulins using multiple contact sites that allow the Ska complex to bind microtubules in multiple modes. Disrupting either the flexibility or the tubulin contact sites of the Ska1 microtubule-binding domain perturbs normal mitotic progression, explaining the critical role of the Ska complex in maintaining a firm grip on dynamic microtubules. PubMed: 24413531DOI: 10.1038/NCOMMS3964 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.01 Å) |
Structure validation
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