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Protein kinase C

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{{#tree:id=OrganizedByTopic|openlevels=0|
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==Conventional PKCs==
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*'''Conventional PKCs'''
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===PKC-a===
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*PKC-a
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[[1dsy]], [[3rdj]], [[3twy]] – rCPKC-α C2 domain – rat
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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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**[[3rdl]], [[4l1l]] - rCPKC-α C2 domain + ion
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[[3gpe]] - rCPKC-α C2 domain + Ca + PTDINS
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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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**[[2eli]] – hCPKC-α C1 domain – human – NMR<br />
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[[4dnl]] - hCPKC-α C2 domain<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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**[[3iw4]] - hCPKC-α kinase domain + inhibitor
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===PKC-β===
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*PKC-β
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[[1a25]] – rCPKC-β C2 domain
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**[[1a25]] – rCPKC-β C2 domain
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===PKC-β2===
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*PKC-β2
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[[2i0e]] - hCPKC-β2 catalytic domain
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**[[2i0e]] - hCPKC-β2 catalytic domain
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[[3pfq]] - rCPKC-β2 (mutant)
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**[[3pfq]] - rCPKC-β2 (mutant)
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===PKC-γ===
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*PKC-γ
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[[2uzp]] - hCPKC-γ C2 domain
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**[[2uzp]] - hCPKC-γ C2 domain
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[[2e73]] - hCPKC-γ C1 domain - NMR
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**[[2e73]] - hCPKC-γ C1 domain - NMR
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[[1tbn]], [[1tbo]] - rCPKC-γ C2 domain – NMR
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**[[1tbn]], [[1tbo]] - rCPKC-γ C2 domain – NMR<br />
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*'''Novel PKC'''
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==Novel PKC==
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*PKC-δ
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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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[[1ptq]] – mNPKC-δ C2 domain – mouse<br />
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**[[1ptr]] - mNPKC-δ C2 domain + phorbol-acetate
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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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[[1bdy]] - rNPKC-δ C2 domain
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**[[1yrk]] – hNPKC-δ C2 domain + peptide
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[[1yrk]] – hNPKC-δ C2 domain + peptide
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**[[2yuu]] - hNPKC-δ C1 domain - NMR
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[[2yuu]] - hNPKC-δ C1 domain - NMR
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**[[2coa]] - hNPKC-δ PH domain – NMR
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[[2coa]] - hNPKC-δ PH domain – NMR
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*PKC-ε
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===PKC-ε===
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**[[1gmi]] – rNPKC-ε C2 domain
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[[1gmi]] – rNPKC-ε C2 domain
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*PKC-τ
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===PKC-τ===
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**[[2enj]] - hNPKC-τ C2 domain – NMR
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[[2enj]] - hNPKC-τ C2 domain – NMR
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**[[2enn]], [[2enz]] - hNPKC-τ C1 domain – NMR
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[[2enn]], [[2enz]] - hNPKC-τ C1 domain – NMR
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**[[1xjd]] – hNPKC-τ + saurosporine
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[[1xjd]] – hNPKC-τ + saurosporine
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**[[2jed]] - hNPKC-τ kinase domain + inhibitor
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[[2jed]] - hNPKC-τ kinase domain + inhibitor
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*PKC-η
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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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[[2fk9]] – hNPKC-η C2 domain<br />
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*PKC-θ
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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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[[4fkd]] – hNPKC-θ second Cys-rich regulatory domain<br />
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*'''Atypical PKC'''
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==Atypical PKC==
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*PKC-ι
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===PKC-ι===
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**[[1vd2]] – hAPKC-ι PB1 domain – NMR
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[[1vd2]] – hAPKC-ι PB1 domain – NMR
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**[[1zrz]] - hAPKC-ι catalytic domain
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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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[[3a8w]], [[3a8x]] - hAPKC-ι kinase domain<br />
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*PKC-ν
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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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-
 
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[[2d9z]] – hPKC-ν PH domain - NMR
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**[[2d9z]] – hPKC-ν PH domain - NMR
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}}
[[Category:Topic Page]]
[[Category:Topic Page]]

Revision as of 11:11, 4 December 2014

Template:STRUCTURE 3gpe

Protein kinase C (PKC) phosphorylate serine or threonine residues in proteins. They act in signal transduction pathways. Conventional PKC (CPKC) - α, β1, β2, γ – are activated by diacylglycerol (DAG), Ca+2 and a phospholipid. Novel PKC (NPKC) – δ, ε, η, θ – are activated by DAG. Atypical (APKC) do not require DAG or Ca+2 for activation. PKC consists of regulatory domain hinged to a catalytic domain. The regulatory domain contains the C1 region which binds 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.

3D structures of protein kinase C

Updated on 04-December-2014

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman, Jaime Prilusky

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