Domain structure of separase and its binding to securin as determined by EM.
Nat Struct Mol Biol
; 12(6): 552-3, 2005 Jun.
Article
in En
| MEDLINE
| ID: mdl-15880121
ABSTRACT
After the degradation of its inhibitor securin, separase initiates chromosome segregation during the metaphase-to-anaphase transition by cleaving cohesin. Here we present a density map at a resolution of 25 A of negatively stained separase-securin complex. Based on labeling data and sequence analysis, we propose a model for the structure of separase, consisting of 26 ARM repeats, an unstructured region of 280 residues and two caspase-like domains, with securin binding to the ARM repeats.
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Database:
MEDLINE
Main subject:
Endopeptidases
/
Cell Cycle Proteins
/
Neoplasm Proteins
Limits:
Humans
Language:
En
Year:
2005
Type:
Article