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| [[Image:3mfr.png|left|200px|thumb|Crystal Structure of membrane associated Ca2+/Calmodulin dependent protein kinase, [[3mfr]]]]
| | <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]])'> |
| {{STRUCTURE_3mfr| PDB=3mfr | SIZE=300| SCENE=CaMKc/Cv/1 |right|CAPTION=Ca2+/Calmodulin dependent protein kinase, [[3mfr]] }}
| | __TOC__ |
| | == Function == |
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| [[Ca2+/Calmodulin dependent protein kinase]] (CaMK) phosphorylates Ser and Thr. It is regulated by Ca2+/[[Calmodulin]] (CaM). It contains an N-terminal catalytic domain, regulatory domain (CBD) and association domain (ASD). CaMKI is a specialized CaM kinase while CaMKII is multifunctional kinase. '''CASK''' is a membrane associated CaMK. '''DAPK''' is a death-associated CaMK which protects cells from some programmed cell death. It contains a regulatory (RD) and autoinhibitory (AD) domains. The images at the left and at the right correspond to one representative CaMK, ''i.e.'' crystal structure of human native membrane associated Ca2+/Calmodulin dependent protein kinase ([[3mfr]]).
| | 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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| {{TOC limit|limit=2}}
| | == Structural highlights == |
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| == 3D Structures of Ca2+/Calmodulin dependent protein kinase == | | 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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| === CaMKI – specialized CaM kinase ===
| | </StructureSection> |
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| | [[Category:Topic Page]] |
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| [[3nyv]] – TgCaMK+WHI-P180 – ''Toxoplasma gondii''<br />
| | ==References== |
| [[3n51]] - TgCaMK CBD +RM-1-95<br />
| | <references/> |
| [[3i7b]] - TgCaMK CBD+ NM-PP1<br />
| | See [[Calcium-dependent protein kinase]] |
| [[3i7c]] - TgCaMK CBD+ NA-PP2<br />
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| [[3ku2]] - TgCaMK CBD<br />
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| [[3khe]], [[3i79]], [[3hzt]] – TgCaMK<br />
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| [[3hx4]] – TgCaMK+Ca<br />
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| [[3dxn]] – TgCaMK kinase domain<br />
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| [[3mwu]] – CpCaMK CBD (mutant)+RM-1-95 – ''Cryptosporidium parvum''<br />
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| [[3ncg]] - CpCaMK CBD + NM-PP1<br />
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| [[3lij]] – CpCaMK+Ca<br />
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| [[3l19]], [[3igo]], [[3hko]] – CpCaMK<br />
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| [[2qg5]] – CpCaMK chains A, B, D<br />
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| [[3f3z]] – CpCaMK kinase domain+indirubin_E804<br />
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| [[3dfa]] - CpCaMK kinase domain<br />
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| [[2aao]] – CaMK chains A, B – ''Arabidopsis thaliana''<br />
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| [[1iq5]] – CeCaMK CBD+XlCaM – ''Xenopus laevis''<br />
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| [[1s6j]] – sCaMK α chain A N-terminal – soybean<br />
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| [[1s6i]] - sCaMK α chain A C-terminal+CaM-like domain<br />
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| [[1mxe]] – rCaMKI CBD+CaM – rat<br />
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| [[1ckk]] – rCaMK CBD chain B+XlCaM<br />
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| [[1a06]] – rCaMK chain A<br />
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| === CASK – membrane-associated CaMK ===
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| [[3mfr]] – hCASK CBD – human<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 /> | |
| [[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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| [[2vz6]] - hCaMKII α chains A, B+ indirubin-E804<br />
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| [[2zv2]] – hCaMKII+STO-609<br />
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| [[2wel]] - hCaMKII δ chain D+CaM<br />
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| [[2w2c]] - hCaMKII δ chain ASD<br />
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| [[2vn9]] - hCaMKII δ chains A-B<br />
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| [[3bhh]] - hCaMKII β chains A-D<br />
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| [[2v7o]] - hCaMKII γ chain A<br />
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| [[2ux0]] - hCaMKII γ (mutant) chains A-F<br />
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| [[2jam]] - hCaMKI γ+peptides<br />
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| [[2jc6]] - hCaMKII δ chains A,C<br />
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| [[1hkx]] - mCaMKII α chains A-N ASD - mouse<br />
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| [[3gp2]] – cCaMKII δ chain B+CaM – chicken<br />
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| [[3kk8]], [[3kk9]] – CeCaMKII – ''Caenorhabditis elegans''<br />
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| [[3kl8]] – CeCaMKII (mutant)+inhibitor<br />
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| [[3ksp]] – CaMKII ASD – ''Exiguobacterium sibiricum''<br />
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| === CaMKIV ===
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| [[2w4o]] – hCaMKIV+inhibitor<br />
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| [[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