Cryo-EM structure of a separase-securin complex at near-atomic resolution

@inproceedings{Boland2017CryoEMSO,
  title={Cryo-EM structure of a separase-securin complex at near-atomic resolution},
  author={Andreas Boland and Thomas R. Martin and Ziguo Zhang and Jing Yang and Xiao-chen Bai and Leifu Chang and Sjors H W Scheres and David Barford},
  booktitle={Nature Structural &Molecular Biology},
  year={2017}
}
Separase is a caspase-family protease that initiates chromatid segregation by cleaving the kleisin subunits (Scc1 and Rec8) of cohesin, and regulates centrosome duplication and mitotic spindle function through cleavage of kendrin and Slk19. To understand the mechanisms of securin regulation of separase, we used single-particle cryo-electron microscopy (cryo-EM) to determine a near-atomic-resolution structure of the Caenorhabditis elegans separase–securin complex. Separase adopts a triangular… CONTINUE READING
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