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4NFA

Structure of the C-terminal doamin of Knl1

Summary for 4NFA
Entry DOI10.2210/pdb4nfa/pdb
Related4NF9
DescriptorProtein CASC5, CHLORIDE ION, GLYCEROL, ... (4 entities in total)
Functional Keywordsrwd domain, cell cycle
Biological sourceHomo sapiens (human)
Cellular locationNucleus: Q8NG31
Total number of polymer chains1
Total formula weight24485.04
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 citationPetrovic, 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: 24530301
DOI: 10.1016/j.molcel.2014.01.019
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.497 Å)
Structure validation

237735

数据于2025-06-18公开中

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