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| </StructureSection> | | </StructureSection> |
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| == 3D Structures of Calcium/calmodulin dependent protein kinase ==
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| Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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| {{#tree:id=OrganizedByTopic|openlevels=0|
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| * CaMKI – specialized CaM kinase
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| **[[1a06]] – rCaMK - rat<br />
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| **[[4fgb]] – hCaMKI - human<br />
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| **[[4fg9]], [[4fg8]], [[4fg7]] – hCaMKI + ATP<br />
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| **[[2jam]] - hCaMKI kinase domain +peptides <br />
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| * CASK – membrane-associated CaMK
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| **[[3mfr]] – hCASK CBD <br />
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| **[[3mfs]] – hCASK+AMPPNP<br />
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| **[[3mft]] – hCASK+Mn<br />
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| **[[3c0g]] – hCASK kinase domain<br />
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| **[[3c0h]] - hCASK kinase domain+AMPPNP<br />
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| **[[3c0i]] - hCASK kinase domain+AMP<br />
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| **[[3tac]] – hCASK kinase domain + liprin-α-2<br />
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| **[[3mfu]] - hCASK+AMPPNP+Mn<br />
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| * DAPK – death-associated CaMK
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| **[[2x0g]] – hDAPK RD+AD+CaM<br />
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| **[[2cke]] – hDAPK+inhibitor<br />
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| * CaMKII – multifunctional CaM kinase
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| **[[3kk9]], [[3kk8]] - hCaMKII kinase domain<br />
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| **[[3soa]] - hCaMKII (mutant)<br />
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| **[[3kl8]] - hCaMKII (mutant) + inhibitor<br />
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| **[[5ig3]] - hCaMKII α chain<br />
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| **[[5hu3]], [[5h9b]], [[5fg8]] - hCaMKII α chain + potassium channel protein EAG<br />
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| **[[2vz6]] - hCaMKII α + indirubin-E804<br />
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| **[[6of8]] - hCaMKII α chain HUB domain (mutant)<br />
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| **[[3bhh]] - hCaMKII β <br />
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| **[[2zv2]] – hCaMKII β +STO-609<br />
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| **[[6hcs]] - hCaMKII β chain + calmodulin<br />
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| **[[2v7o]] - hCaMKII γ <br />
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| **[[2ux0]] - hCaMKII γ (mutant) <br />
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| **[[2wel]] - hCaMKII δ + CaM<br />
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| **[[2w2c]] - hCaMKII δ oligomerization domain<br />
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| **[[2vn9]] - hCaMKII δ <br />
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| **[[2jc6]] - hCaMKII δ <br />
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| **[[6ayw]], [[5vlo]] - hCaMKII δ chain + inhibitor<br />
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| **[[1hkx]] - mCaMKII α - mouse<br />
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| **[[6bab]] - mCaMKII δ chain + inhibitor<br />
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| **[[5u6y]] - rCaMKII α chain<br />
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| **[[3gp2]] – cCaMKII δ + CaM – chicken<br />
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| * CaMKIV
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| **[[2w4o]] – hCaMKIV+inhibitor<br />
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| }}
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| [[Category:Topic Page]] | | [[Category:Topic Page]] |
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FunctionCa2+/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 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]
3D Structures of Calcium/calmodulin dependent protein kinaseCalcium/calmodulin dependent protein kinase 3D structures
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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