Notes on a 2000 JBC paper dissecting the autoinhibitory mechanism of CaMKK, identifying Ile441 as critical for maintaining the inactive state, and showing that CaM-binding peptide orientation does not dictate relief from autoinhibition — a pivotal insight into CaMKK regulation.
Notes on a 2000 JBC paper dissecting the autoinhibitory mechanism of CaMKK, identifying Ile441 as critical for maintaining the inactive state, and showing that CaM-binding peptide orientation does not dictate relief from autoinhibition — a pivotal insight into CaMKK regulation.
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.
Notes on 1998 Cell review discussing kinase phosphoryl transfer mechanisms, conformational dynamics, cofactor roles, and binding motifs. Highlights the debate between associative (SN2) and dissociative (SN1) pathways, with structural evidence for both models.
Notes on 1998 Cell review discussing kinase phosphoryl transfer mechanisms, conformational dynamics, cofactor roles, and binding motifs. Highlights the debate between associative (SN2) and dissociative (SN1) pathways, with structural evidence for both models.
A landmark review on the ordered, site-specific phosphorylation events governing the maturation, activation, and regulation of ABC kinases — using PKC as a paradigm — with profound insights into kinase life cycles, structural stabilization, and multi-step control mechanisms.
A landmark review on the ordered, site-specific phosphorylation events governing the maturation, activation, and regulation of ABC kinases — using PKC as a paradigm — with profound insights into kinase life cycles, structural stabilization, and multi-step control mechanisms.
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 2011 ACS Biochemistry study showing that CaMKKβ, unlike CaMKKα, achieves high autonomous activity via intramolecular autophosphorylation at Thr482, partially releasing itself from autoinhibition and making it Ca2+/CaM-independent — revealing a unique kinase regulation mechanism within the CaMKK family.
Notes on a 2011 ACS Biochemistry study showing that CaMKKβ, unlike CaMKKα, achieves high autonomous activity via intramolecular autophosphorylation at Thr482, partially releasing itself from autoinhibition and making it Ca2+/CaM-independent — revealing a unique kinase regulation mechanism within the CaMKK family.
Note on the detailed structural study of CDPK activation, focusing on apicomplexan CAD conformations (CpCDPK, PfCDPK3), offering new insight into a potentially universal activation mechanism for CDPKs.
Note on the detailed structural study of CDPK activation, focusing on apicomplexan CAD conformations (CpCDPK, PfCDPK3), offering new insight into a potentially universal activation mechanism for CDPKs.
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.
