8Q5H
Human KMN network (outer kinetochore)
Summary for 8Q5H
| Entry DOI | 10.2210/pdb8q5h/pdb |
| EMDB information | 18179 |
| Descriptor | Kinetochore protein Spc24, Kinetochore protein Spc25, Protein MIS12 homolog, ... (7 entities in total) |
| Functional Keywords | outer kinetochore, kmn, complex, cell cycle |
| Biological source | Homo sapiens (human) More |
| Total number of polymer chains | 7 |
| Total formula weight | 185973.55 |
| Authors | Raisch, T.,Polley, S.,Vetter, I.,Musacchio, A.,Raunser, S. (deposition date: 2023-08-09, release date: 2024-02-14, Last modification date: 2024-09-04) |
| Primary citation | Polley, S.,Raisch, T.,Ghetti, S.,Korner, M.,Terbeck, M.,Grater, F.,Raunser, S.,Aponte-Santamaria, C.,Vetter, I.R.,Musacchio, A. Structure of the human KMN complex and implications for regulation of its assembly. Nat.Struct.Mol.Biol., 31:861-873, 2024 Cited by PubMed Abstract: Biorientation of chromosomes during cell division is necessary for precise dispatching of a mother cell's chromosomes into its two daughters. Kinetochores, large layered structures built on specialized chromosome loci named centromeres, promote biorientation by binding and sensing spindle microtubules. One of the outer layer main components is a ten-subunit assembly comprising Knl1C, Mis12C and Ndc80C (KMN) subcomplexes. The KMN is highly elongated and docks on kinetochores and microtubules through interfaces at its opposite extremes. Here, we combine cryogenic electron microscopy reconstructions and AlphaFold2 predictions to generate a model of the human KMN that reveals all intra-KMN interfaces. We identify and functionally validate two interaction interfaces that link Mis12C to Ndc80C and Knl1C. Through targeted interference experiments, we demonstrate that this mutual organization strongly stabilizes the KMN assembly. Our work thus reports a comprehensive structural and functional analysis of this part of the kinetochore microtubule-binding machinery and elucidates the path of connections from the chromatin-bound components to the force-generating components. PubMed: 38459128DOI: 10.1038/s41594-024-01230-9 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.5 Å) |
Structure validation
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