4NFA
Structure of the C-terminal doamin of Knl1
Summary for 4NFA
Entry DOI | 10.2210/pdb4nfa/pdb |
Related | 4NF9 |
Descriptor | Protein CASC5, CHLORIDE ION, GLYCEROL, ... (4 entities in total) |
Functional Keywords | rwd domain, cell cycle |
Biological source | Homo sapiens (human) |
Cellular location | Nucleus: Q8NG31 |
Total number of polymer chains | 1 |
Total formula weight | 24485.04 |
Authors | Petrovic, A.,Mosalaganti, S.,Keller, J.,Mattiuzzo, M.,Overlack, K.,Wohlgemuth, S.,Pasqualato, S.,Raunser, S.,Musacchio, A. (deposition date: 2013-10-31, release date: 2014-03-19, Last modification date: 2024-02-28) |
Primary citation | Petrovic, A.,Mosalaganti, S.,Keller, J.,Mattiuzzo, M.,Overlack, K.,Krenn, V.,De Antoni, A.,Wohlgemuth, S.,Cecatiello, V.,Pasqualato, S.,Raunser, S.,Musacchio, A. Modular Assembly of RWD Domains on the Mis12 Complex Underlies Outer Kinetochore Organization. Mol.Cell, 53:591-605, 2014 Cited by PubMed Abstract: Faithful chromosome segregation is mandatory for cell and organismal viability. Kinetochores, large protein assemblies embedded in centromeric chromatin, establish a mechanical link between chromosomes and spindle microtubules. The KMN network, a conserved 10-subunit kinetochore complex, harbors the microtubule-binding interface. RWD domains in the KMN subunits Spc24 and Spc25 mediate kinetochore targeting of the microtubule-binding subunits by interacting with the Mis12 complex, a KMN subcomplex that tethers directly onto the underlying chromatin layer. Here, we show that Knl1, a KMN subunit involved in mitotic checkpoint signaling, also contains RWD domains that bind the Mis12 complex and that mediate kinetochore targeting of Knl1. By reporting the first 3D electron microscopy structure of the KMN network, we provide a comprehensive framework to interpret how interactions of RWD-containing proteins with the Mis12 complex shape KMN network topology. Our observations unveil a regular pattern in the construction of the outer kinetochore. PubMed: 24530301DOI: 10.1016/j.molcel.2014.01.019 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.497 Å) |
Structure validation
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