3VZ9
Crystal structure of the chicken Spc24-Spc25 globular domain
Summary for 3VZ9
| Entry DOI | 10.2210/pdb3vz9/pdb |
| Related | 3VZA |
| Descriptor | Uncharacterized protein, Spc24 protein (3 entities in total) |
| Functional Keywords | rwd domain, kinetochore component, chromosome segregation, ndc80 complex, cell cycle |
| Biological source | Gallus gallus (chicken) More |
| Total number of polymer chains | 2 |
| Total formula weight | 20994.58 |
| Authors | Nishino, T.,Fukagawa, T. (deposition date: 2012-10-09, release date: 2013-04-03, Last modification date: 2023-11-08) |
| Primary citation | Nishino, T.,Rago, F.,Hori, T.,Tomii, K.,Cheeseman, I.M.,Fukagawa, T. CENP-T provides a structural platform for outer kinetochore assembly Embo J., 32:424-436, 2013 Cited by PubMed Abstract: The kinetochore forms a dynamic interface with microtubules from the mitotic spindle during mitosis. The Ndc80 complex acts as the key microtubule-binding complex at kinetochores. However, it is unclear how the Ndc80 complex associates with the inner kinetochore proteins that assemble upon centromeric chromatin. Here, based on a high-resolution structural analysis, we demonstrate that the N-terminal region of vertebrate CENP-T interacts with the 'RWD' domain in the Spc24/25 portion of the Ndc80 complex. Phosphorylation of CENP-T strengthens a cryptic hydrophobic interaction between CENP-T and Spc25 resulting in a phospho-regulated interaction that occurs without direct recognition of the phosphorylated residue. The Ndc80 complex interacts with both CENP-T and the Mis12 complex, but we find that these interactions are mutually exclusive, supporting a model in which two distinct pathways target the Ndc80 complex to kinetochores. Our results provide a model for how the multiple protein complexes at kinetochores associate in a phospho-regulated manner. PubMed: 23334297DOI: 10.1038/emboj.2012.348 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.03 Å) |
Structure validation
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