Activation segment exchange: a common mechanism of kinase autophosphorylation?
The crystal structure of the kinase domain from human checkpoint kinase 2 (Chk2) has shown, for the first time, the reciprocal exchange of activation segments between two adjacent molecules and provides the molecular basis for understanding the observed mode of Chk2 kinase activation via trans-autop...
Main Authors: | Oliver, A, Knapp, S, Pearl, L |
---|---|
Format: | Journal article |
Language: | English |
Published: |
2007
|
Similar Items
-
Activation segment dimerization: a mechanism for kinase autophosphorylation of non-consensus sites
by: Pike, A, et al.
Published: (2008) -
Activation segment dimerization: a mechanism for kinase autophosphorylation of non-consensus sites.
by: Pike, A, et al.
Published: (2008) -
Autophosphorylation restrains the apoptotic activity of DRP-1 kinase by controlling dimerization and calmodulin binding.
by: Shani, G, et al.
Published: (2001) -
Helix Bundle Loops Determine Whether Histidine Kinases Autophosphorylate in cis or in trans
by: Ashenberg, Orr, et al.
Published: (2016) -
Tyro3 carboxyl terminal region confers stability and contains the autophosphorylation sites
by: Shao, Hanshuang, et al.
Published: (2018)