The CaMKII Holoenzyme Structure in Activation-Competent Conformation

Notes on a 2017 Nature Communications paper revealing the 3D structure of the CaMKII holoenzyme in an activation-competent conformation, emphasizing the role of flexible linkers and dimeric kinase domain interactions in regulating activation and frequency decoding.

The CaMKII Holoenzyme Structure in Activation-Competent Conformation

Notes on a 2017 Nature Communications paper revealing the 3D structure of the CaMKII holoenzyme in an activation-competent conformation, emphasizing the role of flexible linkers and dimeric kinase domain interactions in regulating activation and frequency decoding.

Membrane Binding of Recoverin: From Mechanistic Understanding to Biological Functionality

A comprehensive study unraveling the molecular dynamics of recoverin’s membrane binding via its calcium-dependent myristoyl switch, highlighting the importance of N-terminal domain conformations and transient C-terminal interactions.

Membrane Binding of Recoverin: From Mechanistic Understanding to Biological Functionality

A comprehensive study unraveling the molecular dynamics of recoverin’s membrane binding via its calcium-dependent myristoyl switch, highlighting the importance of N-terminal domain conformations and transient C-terminal interactions.

N-terminal Domain of CDPK1 Determines Substrate Specificity: A Key to Rewiring Kinase Signaling

Note on the discovery that the variable N-terminal domain of CDPK1 controls substrate specificity—offering a new mechanism to engineer signaling specificity in plants.

N-terminal Domain of CDPK1 Determines Substrate Specificity: A Key to Rewiring Kinase Signaling

Note on the discovery that the variable N-terminal domain of CDPK1 controls substrate specificity—offering a new mechanism to engineer signaling specificity in plants.

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