Protein kinase C

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<StructureSection load='3gpe' size='350' side='right' caption='Rat protein kinase α C2 domain complex with phosphatidylinositol, phosphate and Ca+2 ion (green), [[3gpe]] ' scene=''>
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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'>
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__TOC__
== Function ==
== Function ==
'''Protein kinase C''' (PKC) phosphorylates serine or threonine residues in proteins. PKC act in signal transduction pathways<ref>PMID:11440359</ref>. PKC consists of regulatory domain hinged to a catalytic domain. The regulatory domain contains the C1 region which binds diacylglycerol (DAG) and phorbol esters and the C2 domain which is a Ca+2 sensor. PKC contains Pleckstrin Homology (PH) domain which binds phosphatidylinositol lipids (PTDINS). The PH domain is found in proteins involved in intracellular signaling.
'''Protein kinase C''' (PKC) phosphorylates serine or threonine residues in proteins. PKC act in signal transduction pathways<ref>PMID:11440359</ref>. PKC consists of regulatory domain hinged to a catalytic domain. The regulatory domain contains the C1 region which binds diacylglycerol (DAG) and phorbol esters and the C2 domain which is a Ca+2 sensor. PKC contains Pleckstrin Homology (PH) domain which binds phosphatidylinositol lipids (PTDINS). The PH domain is found in proteins involved in intracellular signaling.
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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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