Calcium/Calmodulin-dependent protein kinase

Function

Ca2+/Calmodulin dependent protein kinase (CaMK) are mammalian calmodulin-dependent calcium-dependent protein kinases activated by elevation of Ca+2 and calmodulin concentration to phosphorylate Ser and Thr.

CaMKI is a specialized CaM kinase.
CaMKII is multifunctional kinase.
CaMKIII phosphorylates eukaryotic elongation factor 2.
CASK is a membrane associated CaMK.
DAPK is a death-associated CaMK which protects cells from some programmed cell death.

For details see Calcium-dependent protein kinase.

Structural highlights

CAMKII contains an N-terminal catalytic domain which binds ATP and substrate protein, regulatory domain (CBD) and association domain (ASD). DAPK contains a regulatory (RD) and autoinhibitory (AD) domains. The activity of human CamKII is regulated by autophosphorylation of and Thr 305 (T305 is not in the pdb file). ^[1]

3D Structures of Calcium/calmodulin dependent protein kinase

Calcium/calmodulin dependent protein kinase 3D structures

Human CamKII subunit α kinase domain complex with indirubin (PDB code 2vz6)

Drag the structure with the mouse to rotate

ReferencesReferences

↑ Rellos P, Pike AC, Niesen FH, Salah E, Lee WH, von Delft F, Knapp S. Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. PLoS Biol. 2010 Jul 27;8(7):e1000426. PMID:20668654 doi:10.1371/journal.pbio.1000426

See Calcium-dependent protein kinase

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Alexander Berchansky, Michal Harel, Alice Harmon, Jaime Prilusky

[1] Rellos P, Pike AC, Niesen FH, Salah E, Lee WH, von Delft F, Knapp S. Structure of the CaMKIIdelta/calmodulin complex reveals the molecular mechanism of CaMKII kinase activation. PLoS Biol. 2010 Jul 27;8(7):e1000426. PMID:20668654 doi:10.1371/journal.pbio.1000426

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