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4CA0

Structural Basis for the microtubule binding of the human kinetochore Ska complex

Summary for 4CA0
Entry DOI10.2210/pdb4ca0/pdb
Related4C9Y
DescriptorSPINDLE AND KINETOCHORE-ASSOCIATED PROTEIN 1 (2 entities in total)
Functional Keywordscell cycle, cell divison, kinetochore-microtubule attachment, winged-helix domain
Biological sourceHOMO SAPIENS (HUMAN)
Cellular locationCytoplasm, cytoskeleton, spindle: Q96BD8
Total number of polymer chains2
Total formula weight29288.22
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, Last modification date: 2024-11-06)
Primary citationAbad, 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: 24413531
DOI: 10.1038/NCOMMS3964
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.259 Å)
Structure validation

227111

數據於2024-11-06公開中

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