Calcium/Calmodulin-dependent protein kinase
From Proteopedia
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| - | [[ | + | <StructureSection load='2vz6' size='350' side='right' scene='41/415817/Cv/2' caption='Human CamKII subunit α kinase domain complex with indirubin (PDB code [[2vz6]])'> |
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| + | == Function == | ||
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| + | 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. <br /> | ||
| + | *'''CaMKI''' is a specialized CaM kinase.<br /> | ||
| + | *'''CaMKII''' is multifunctional kinase. <br /> | ||
| + | *'''CaMKIII''' phosphorylates eukaryotic elongation factor 2. <br /> | ||
| + | *'''CASK''' is a membrane associated CaMK.<br /> | ||
| + | *'''DAPK''' is a death-associated CaMK which protects cells from some programmed cell death. <br /> | ||
| + | For details see [[Calcium-dependent protein kinase]]. | ||
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| + | == Structural highlights == | ||
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| + | 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 <scene name='41/415817/Cv/3'>Thr 286</scene> and Thr 305 (T305 is not in the pdb file). <ref>PMID:20668654</ref> | ||
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| + | == 3D Structures of Calcium/calmodulin dependent protein kinase == | ||
| + | [[Calcium/calmodulin dependent protein kinase 3D structures]] | ||
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| + | </StructureSection> | ||
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| + | [[Category:Topic Page]] | ||
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| + | ==References== | ||
| + | <references/> | ||
| + | See [[Calcium-dependent protein kinase]] | ||
Current revision
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References
- ↑ 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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