Notes on a 2011 Cell paper that reveals the full-length crystal structure of human CaMKII in its autoinhibited state and introduces a tunable mechanism for calcium signal decoding based on linker length-dependent conformational dynamics.
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 landmark Nature (1999) paper detailing how calmodulin (CaM) adopts a unique binding mode when interacting with CaMKK, revealing an extended 26-residue peptide interface and an opposite binding orientation, distinguishing it from classical CaM-target interactions — a new paradigm in calcium signaling complexes.
Notes on a landmark Nature (1999) paper detailing how calmodulin (CaM) adopts a unique binding mode when interacting with CaMKK, revealing an extended 26-residue peptide interface and an opposite binding orientation, distinguishing it from classical CaM-target interactions — a new paradigm in calcium signaling complexes.
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.
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.
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.
A 1975 Science paper pioneering the computational prediction of EF-hand calcium-binding motifs in unexpected proteins, revealing evolutionary insights into calcium sensor domains and highlighting structural conservation even in non-calcium-binding proteins.
A 1975 Science paper pioneering the computational prediction of EF-hand calcium-binding motifs in unexpected proteins, revealing evolutionary insights into calcium sensor domains and highlighting structural conservation even in non-calcium-binding proteins.
