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Literature summary extracted from

  • Hoffman, L.; Stein, R.A.; Colbran, R.J.; Mchaourab, H.S.
    Conformational changes underlying calcium/calmodulin-dependent protein kinase II activation (2011), EMBO J., 30, 1251-1262.
    View publication on PubMedView publication on EuropePMC

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.11.17 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
2.7.11.17 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(Commentary)

EC Number Cloned (Comment) Organism
2.7.11.17 expression in Escherichia coli Caenorhabditis elegans
2.7.11.17 expression in Sf9 cells Mus musculus

Protein Variants

EC Number Protein Variants Comment Organism
2.7.11.17 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

EC Number Inhibitors Comment Organism Structure
2.7.11.17 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
2.7.11.17 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

EC Number Organism UniProt Comment Textmining
2.7.11.17 Caenorhabditis elegans O62305
-
-
2.7.11.17 Mus musculus P11798
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.11.17
-
 Mus musculus
2.7.11.17
-
 Caenorhabditis elegans

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.11.17 ATP + autocamtide-2 highly selective peptide substrate for calcium/calmodulin-dependent protein kinase II Mus musculus ADP + phosphorylated autocamtide-2
-
 ?
2.7.11.17 ATP + autocamtide-2 highly selective peptide substrate for calcium/calmodulin-dependent protein kinase II Caenorhabditis elegans ADP + phosphorylated autocamtide-2
-
 ?
2.7.11.17 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
-
 ?
2.7.11.17 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

EC Number Synonyms Comment Organism
2.7.11.17 CaMKII
-
 Caenorhabditis elegans
2.7.11.17 CaMKIIalpha
-
 Mus musculus