Article
A new Mad2-interacting domain of Cdc20 is critical for the function of Mad2-Cdc20 complex in the spindle assembly checkpoint.
The Biochemical journal - 1 Jun 2006
Mondal Gourish, Baral Rathindra N, Roychoudhury Susanta
This publication is marked as retracted by the source.
Abstract excerpt
Interaction between Mad2 and Cdc20 (cell division cycle 20) is a key event during spindle assembly checkpoint activation. In the past, an N-terminal peptide containing amino acid residues 111-150 of Cdc20 was shown to bind Mad2 much better than the full-length Cdc20 protein. Using co-localization, co-immunoprecipitation and peptide inhibition analysis with different deletion mutants of Cdc20, we identified...
Read the complete abstract on PubMedTopics
- Amino Acid Motifs
- Amino Acid Sequence
- Animals
- Binding Sites
- Calcium-Binding Proteins
