F-Helix as a Structural Scaffold for Active Protein Kinase Assembly

Notes on 2008_PNAS paper revealing F-helix as a hub for regulatory and catalytic spine anchoring in protein kinases.

F-Helix as a Structural Scaffold for Active Protein Kinase Assembly

Notes on 2008_PNAS paper revealing F-helix as a hub for regulatory and catalytic spine anchoring in protein kinases.

Mechanism of CDK Activation Revealed by the Structure of a CyclinA-CDK2 Complex

Notes on a 1995 Nature paper revealing the structural mechanism of CDK2 activation by cyclinA, focusing on key conformational changes that relieve autoinhibition and organize the catalytic site.

Mechanism of CDK Activation Revealed by the Structure of a CyclinA-CDK2 Complex

Notes on a 1995 Nature paper revealing the structural mechanism of CDK2 activation by cyclinA, focusing on key conformational changes that relieve autoinhibition and organize the catalytic site.

Allosteric Activation of Toxoplasma CDPK1: A Splint Model for Kinase Regulation

A fascinating study revealing that TgCDPK1 is stabilized and activated via an allosteric mechanism involving its regulatory CAD domain, challenging classical models of calcium-dependent kinase activation.

Allosteric Activation of Toxoplasma CDPK1: A Splint Model for Kinase Regulation

A fascinating study revealing that TgCDPK1 is stabilized and activated via an allosteric mechanism involving its regulatory CAD domain, challenging classical models of calcium-dependent kinase activation.

Structural Insights into Apicomplexan CDPK Activation: A Calcium-Triggered Mechanism

A landmark structural study revealing how apicomplexan CDPKs (TgCDPK1/3, CpCDPK) undergo dramatic conformational changes upon calcium binding to shift from an autoinhibited to an active state.

Structural Insights into Apicomplexan CDPK Activation: A Calcium-Triggered Mechanism

A landmark structural study revealing how apicomplexan CDPKs (TgCDPK1/3, CpCDPK) undergo dramatic conformational changes upon calcium binding to shift from an autoinhibited to an active state.

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.

Target-Induced Conformational Adaptation of Calmodulin in Complex with Nematode CaMKK Peptide: Insights into Calcium-Dependent Kinase Regulation

Notes on a 2001 Journal of Molecular Biology paper revealing the crystal structure of Ca2+/CaM bound to a CaMKK-derived peptide, highlighting how calmodulin achieves conformational flexibility to accommodate diverse targets — offering a mechanistic basis for how CaM relieves autoinhibition of kinases like CaMKK and mediates calcium signal transduction.

Target-Induced Conformational Adaptation of Calmodulin in Complex with Nematode CaMKK Peptide: Insights into Calcium-Dependent Kinase Regulation

Notes on a 2001 Journal of Molecular Biology paper revealing the crystal structure of Ca2+/CaM bound to a CaMKK-derived peptide, highlighting how calmodulin achieves conformational flexibility to accommodate diverse targets — offering a mechanistic basis for how CaM relieves autoinhibition of kinases like CaMKK and mediates calcium signal transduction.

Autophosphorylation-Dependent Activation of a Calcium-Dependent Protein Kinase from Groundnut

Notes on a 1999 ASPS paper analyzing autophosphorylation-dependent activation of a calcium-dependent protein kinase (GnCDPK) from groundnut and its role in substrate phosphorylation.

Autophosphorylation-Dependent Activation of a Calcium-Dependent Protein Kinase from Groundnut

Notes on a 1999 ASPS paper analyzing autophosphorylation-dependent activation of a calcium-dependent protein kinase (GnCDPK) from groundnut and its role in substrate phosphorylation.

A Critical Evolution of Protein Kinase Regulation by Activation Loop Autophosphorylation

Notes on the 2023 eLife review analyzing protein kinase activation loop autophosphorylation. Discusses cis vs. trans mechanisms, dimerization, regulation, and the biochemical, structural, and kinetic evidence for these processes, while addressing the enigmatic nature of autophosphorylation.

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