Calcium/Calmodulin-dependent protein kinase: Difference between revisions
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== Structural highlights == | == 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 <scene name='41/415817/Cv/3'>Thr 286</scene> and Thr 305 (T305 is not in the pdb file). | 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> | ||
</StructureSection> | </StructureSection> | ||
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==References== | ==References== | ||
<references/> | |||
See [[Calcium-dependent protein kinase]] | See [[Calcium-dependent protein kinase]] |
Revision as of 16:11, 17 November 2015
FunctionCa2+/Calmodulin dependent protein kinase (CaMK) are activated by elevation of Ca+2 and calmodulin concentration to phosphorylate Ser and Thr.
For details see Calcium-dependent protein kinase. Structural highlightsCAMKII 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]
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3D Structures of Ca2+/Calmodulin dependent protein kinase3D Structures of Ca2+/Calmodulin dependent protein kinase
Updated on 17-November-2015
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