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Protein kinase C

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<StructureSection load='3gpe' size='400' side='right' caption='Rat protein kinase α C2 domain complex with phosphatidylinositol, phosphate and Ca+2 ion (green), [[3gpe]] ' scene='46/468129/Cv/1'>
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<StructureSection load='' size='350' side='right' caption='Rat protein kinase α C2 domain complex with phosphatidylinositol, phosphate and Ca+2 ion (green), [[3gpe]] ' scene='46/468129/Cv/1'>
__TOC__
__TOC__
== Function ==
== Function ==
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== Structural highlights ==
== Structural highlights ==
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Phosphatidylinositol binds to PKC-α C2 domain groove near the Ca+2 binding pocket<ref>PMID:19346474</ref>.
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<scene name='46/468129/Cv/6'>Phosphatidylinositol binds to PKC-α C2 domain groove</scene> near the <scene name='46/468129/Cv/7'>Ca+2 binding pocket</scene><ref>PMID:19346474</ref>. Water molecules are shown as red spheres.
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</StructureSection>
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==3D structures of protein kinase C==
==3D structures of protein kinase C==
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[[Protein kinase C 3D structures]]
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
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</StructureSection>
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{{#tree:id=OrganizedByTopic|openlevels=0|
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*'''Conventional PKCs'''
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*PKC-α
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**[[1dsy]], [[3rdj]], [[3twy]] – rCPKC-α C2 domain – rat
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**[[3rdl]], [[4l1l]] - rCPKC-α C2 domain + ion
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**[[3gpe]] - rCPKC-α C2 domain + Ca + PTDINS
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**[[2eli]] – hCPKC-α C1 domain – human – NMR<br />
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**[[4dnl]] - hCPKC-α C2 domain<br />
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**[[3iw4]] - hCPKC-α kinase domain + inhibitor
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*PKC-β
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**[[1a25]] – rCPKC-β C2 domain
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*PKC-β2
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**[[2i0e]] - hCPKC-β2 catalytic domain
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**[[3pfq]] - rCPKC-β2 (mutant)
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*PKC-γ
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**[[2uzp]] - hCPKC-γ C2 domain
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**[[2e73]] - hCPKC-γ C1 domain - NMR
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**[[1tbn]], [[1tbo]] - rCPKC-γ C2 domain – NMR<br />
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*'''Novel PKC'''
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*PKC-δ
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**[[1ptq]] – mNPKC-δ C2 domain – mouse<br />
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**[[3uej]] - mNPKC-δ C1B domain<br />
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**[[3uey]], [[3uff]], [[3ugd]], [[3ugi]], [[3ugl]] - mNPKC-δ C1B domain (mutant)<br />
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**[[1ptr]] - mNPKC-δ C2 domain + phorbol-acetate
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**[[1bdy]] - rNPKC-δ C2 domain
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**[[1yrk]] – hNPKC-δ C2 domain + peptide
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**[[2yuu]] - hNPKC-δ C1 domain - NMR
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**[[2coa]] - hNPKC-δ PH domain – NMR
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*PKC-ε
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**[[1gmi]] – rNPKC-ε C2 domain
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*PKC-η
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**[[2fk9]] – hNPKC-η C2 domain<br />
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**[[3txo]] - hNPKC-η kinase domain (mutant) + inhibitor<br />
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*PKC-θ
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**[[4fkd]] – hNPKC-θ second Cys-rich regulatory domain<br />
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**[[2enj]] - hNPKC-θ C2 domain – NMR
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**[[2enn]], [[2enz]] - hNPKC-θ C1 domain – NMR
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**[[1xjd]] – hNPKC-θ + saurosporine
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**[[2jed]] - hNPKC-θ kinase domain + inhibitor
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*'''Atypical PKC'''
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*PKC-ι
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**[[1vd2]] – hAPKC-ι PB1 domain – NMR
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**[[1zrz]] - hAPKC-ι catalytic domain
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**[[3a8w]], [[3a8x]] - hAPKC-ι kinase domain<br />
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**[[3zh8]] - hAPKC-ι kinase domain (mutant) + inhibitor<br />
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**[[1wmh]] - hAPKC-ι PB1 domain + PAR6 alpha<br />
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**[[4dc2]] - hAPKC-ι residues 231-595 + PAR3 peptide<br />
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*PKC-ν
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**[[2d9z]] – hPKC-ν PH domain - NMR
 
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}}
 
== References ==
== References ==
<references/>
<references/>
[[Category:Topic Page]]
[[Category:Topic Page]]

Current revision

Rat protein kinase α C2 domain complex with phosphatidylinositol, phosphate and Ca+2 ion (green), 3gpe

Drag the structure with the mouse to rotate

References

  1. ↑ Idris I, Gray S, Donnelly R. Protein kinase C activation: isozyme-specific effects on metabolism and cardiovascular complications in diabetes. Diabetologia. 2001 Jun;44(6):659-73. PMID:11440359 doi:http://dx.doi.org/10.1007/s001250051675
  2. ↑ Koya D, King GL. Protein kinase C activation and the development of diabetic complications. Diabetes. 1998 Jun;47(6):859-66. PMID:9604860
  3. ↑ Koivunen J, Aaltonen V, Peltonen J. Protein kinase C (PKC) family in cancer progression. Cancer Lett. 2006 Apr 8;235(1):1-10. PMID:15907369 doi:http://dx.doi.org/10.1016/j.canlet.2005.03.033
  4. ↑ Guerrero-Valero M, Ferrer-Orta C, Querol-Audi J, Marin-Vicente C, Fita I, Gomez-Fernandez JC, Verdaguer N, Corbalan-Garcia S. Structural and mechanistic insights into the association of PKC{alpha}-C2 domain to PtdIns(4,5)P2. Proc Natl Acad Sci U S A. 2009 Apr 3. PMID:19346474

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