Image the Mec1-Ddc2 complex at 3.9 ångströms (VIDEO)
Caption
Each Mec1-Ddc2 complex contains two copies of Mec1 and two copies of Ddc2. The dimeric architecture resembles a butterfly stretching out its wings The structure illuminates critical regulatory sites of the ATR kinase, which are highly conserved among kinase family. Without DNA damage or replication stress, the in vivo Mec1-Ddc2 is poised for catalysis, due to the inhibition on the activation loop. Specific Mec1/ATR activators could immediately release the inhibition on the activation loop and culminate in full ATR kinase activity.
Credit
©University of Science and Technology of China By Gang Cai and Xuejuan Wang
Usage Restrictions
None
License
Licensed content