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