Calcium/Calmodulin-dependent protein kinase

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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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__TOC__
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== Function ==
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{{STRUCTURE_3mfr| PDB=3mfr | SIZE=400| SCENE=CaMKc/Cv/1 |right|CAPTION=Ca2+/Calmodulin dependent protein kinase complex with phosphoaminophosphonic acid-adenylate ester, [[3mfr]] }}
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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 />
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*'''CaMKI''' is a specialized CaM kinase.<br />
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*'''CaMKII''' is multifunctional kinase. <br />
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*'''CaMKIII''' phosphorylates eukaryotic elongation factor 2. <br />
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*'''CASK''' is a membrane associated CaMK.<br />
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*'''DAPK''' is a death-associated CaMK which protects cells from some programmed cell death. <br />
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For details see [[Calcium-dependent protein kinase]].
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[[Ca2+/Calmodulin dependent protein kinase]] (CaMK) phosphorylates Ser and Thr. It is regulated by Ca<sup>2+</sup>/[[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 Ca<sup>2+</sup>/Calmodulin dependent protein kinase ([[3mfr]]).
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== Structural highlights ==
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== 3D Structures of Ca<sup>2+</sup>/Calmodulin dependent protein kinase ==
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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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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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== 3D Structures of Calcium/calmodulin dependent protein kinase ==
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[[Calcium/calmodulin dependent protein kinase 3D structures]]
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=== CaMKK – CaM kinase kinase ===
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</StructureSection>
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[[1iq5]] – CeCaMK CBD+XlCaM – ''Xenopus laevis''<br />
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=== CaMKI – specialized CaM kinase ===
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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 />
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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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[[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]]
[[Category:Topic Page]]
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==See also==
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==References==
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<references/>
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[[Calcium-dependent protein kinase]], a member of the CaM kinase family
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See [[Calcium-dependent protein kinase]]

Current revision

Human CamKII subunit α kinase domain complex with indirubin (PDB code 2vz6)

Drag the structure with the mouse to rotate

References

  1. ↑ 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

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