Activating Compound | Comment | Organism | Structure |
---|---|---|---|
additional information | autoinhibition and activation of the kinase domain of CaMKII. Autoinhibition involves a conformeric equilibrium of the regulatory domain, modulating substrate and nucleotide access. Binding of calmodulin to the regulatory domain induces conformational changes that release the catalytic cleft, activating the kinase and exposing an otherwise inaccessible phosphorylation site, threonine 286. Autophosphorylation at Thr286 further disrupts the interactions between the catalytic and regulatory domains, enhancing the interaction with calmodulin, but maintains the regulatory domain in a dynamic unstructured conformation following dissociation of calmodulin, sustaining activation | Mus musculus | |
additional information | autoinhibition and activation of the kinase domain of CaMKII. Autoinhibition involves a conformeric equilibrium of the regulatory domain, modulating substrate and nucleotide access. Binding of calmodulin to the regulatory domain induces conformational changes that release the catalytic cleft, activating the kinase and exposing an otherwise inaccessible phosphorylation site, threonine 286. Autophosphorylation at Thr286 further disrupts the interactions between the catalytic and regulatory domains, enhancing the interaction with calmodulin, but maintains the regulatory domain in a dynamic unstructured conformation following dissociation of calmodulin, sustaining activation | Caenorhabditis elegans |
Cloned (Comment) | Organism |
---|---|
expression in Escherichia coli | Caenorhabditis elegans |
expression in Sf9 cells | Mus musculus |
Protein Variants | Comment | Organism |
---|---|---|
T286E/D135N | phosphomimic mutant, lower melting temperature. Distinct changes in backbone order upon binding of Ca2+/CaM to the T286E/D135N mutant | Caenorhabditis elegans |
Inhibitors | Comment | Organism | Structure |
---|---|---|---|
additional information | autoinhibition and activation of the kinase domain of CaMKII. Autoinhibition involves a conformeric equilibrium of the regulatory domain, modulating substrate and nucleotide access. Binding of calmodulin to the regulatory domain induces conformational changes that release the catalytic cleft, activating the kinase and exposing an otherwise inaccessible phosphorylation site, threonine 286. Autophosphorylation at Thr286 further disrupts the interactions between the catalytic and regulatory domains, enhancing the interaction with calmodulin, but maintains the regulatory domain in a dynamic unstructured conformation following dissociation of calmodulin, sustaining activation | Caenorhabditis elegans | |
additional information | autoinhibition and activation of the kinase domain of CaMKII. Autoinhibition involves a conformeric equilibrium of the regulatory domain, modulating substrate and nucleotide access. Binding of calmodulin to the regulatory domain induces conformational changes that release the catalytic cleft, activating the kinase and exposing an otherwise inaccessible phosphorylation site, threonine 286. Autophosphorylation at Thr286 further disrupts the interactions between the catalytic and regulatory domains, enhancing the interaction with calmodulin, but maintains the regulatory domain in a dynamic unstructured conformation following dissociation of calmodulin, sustaining activation | Mus musculus |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Caenorhabditis elegans | O62305 | - |
- |
Mus musculus | P11798 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Mus musculus |
- |
Caenorhabditis elegans |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
ATP + autocamtide-2 | highly selective peptide substrate for calcium/calmodulin-dependent protein kinase II | Mus musculus | ADP + phosphorylated autocamtide-2 | - |
? | |
ATP + autocamtide-2 | highly selective peptide substrate for calcium/calmodulin-dependent protein kinase II | Caenorhabditis elegans | ADP + phosphorylated autocamtide-2 | - |
? | |
ATP + syntide-2 | a peptide containing the R-X-X-S/T consensus phosphorylation site 2 of glycogen synthase within the sequence | Mus musculus | ADP + phosphorylated syntide-2 | - |
? | |
ATP + syntide-2 | a peptide containing the R-X-X-S/T consensus phosphorylation site 2 of glycogen synthase within the sequence | Caenorhabditis elegans | ADP + phosphorylated syntide-2 | - |
? |
Synonyms | Comment | Organism |
---|---|---|
CaMKII | - |
Caenorhabditis elegans |
CaMKIIalpha | - |
Mus musculus |