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