Protein kinase C: Difference between revisions
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{{STRUCTURE_3gpe| PDB=3gpe | SIZE=400| SCENE= |right|CAPTION=Rat protein kinase a C2 domain complex with phosphatidylinositol and Ca+2 ion, [[3gpe]] }} | {{STRUCTURE_3gpe| PDB=3gpe | SIZE=400| SCENE= |right|CAPTION=Rat protein kinase a C2 domain complex with phosphatidylinositol and Ca+2 ion, [[3gpe]] }} | ||
'''Protein kinase C''' (PKC) phosphorylate serine or threonine residues in proteins. They act in signal transduction pathways. Conventional PKC (CPKC) - | '''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. | ||
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===PKC-a=== | ===PKC-a=== | ||
[[1dsy]], [[3rdj]] – rCPKC- | [[1dsy]], [[3rdj]] – rCPKC-α C2 domain – rat | ||
[[3rdl]] - rCPKC- | [[3rdl]] - rCPKC-α C2 domain + Pb | ||
[[3gpe]] - rCPKC- | [[3gpe]] - rCPKC-α C2 domain + Ca + PTDINS | ||
[[2eli]] – hCPKC- | [[2eli]] – hCPKC-α C1 domain – human – NMR | ||
[[3iw4]] - hCPKC- | [[3iw4]] - hCPKC-α kinase domain + inhibitor | ||
===PKC- | ===PKC-β=== | ||
[[1a25]] – rCPKC- | [[1a25]] – rCPKC-β C2 domain | ||
===PKC- | ===PKC-β2=== | ||
[[2i0e]] - hCPKC- | [[2i0e]] - hCPKC-β2 catalytic domain | ||
[[3pfq]] - rCPKC- | [[3pfq]] - rCPKC-β2 (mutant) | ||
===PKC- | ===PKC-γ=== | ||
[[2uzp]] - hCPKC- | [[2uzp]] - hCPKC-γ C2 domain | ||
[[2e73]] - hCPKC- | [[2e73]] - hCPKC-γ C1 domain - NMR | ||
[[1tbn]], [[1tbo]] - rCPKC- | [[1tbn]], [[1tbo]] - rCPKC-γ C2 domain – NMR | ||
==Novel PKC== | ==Novel PKC== | ||
===PKC- | ===PKC-δ=== | ||
[[1ptq]] – mNPKC- | [[1ptq]] – mNPKC-δ C2 domain – mouse | ||
[[1ptr]] - mNPKC- | [[1ptr]] - mNPKC-δ C2 domain + phorbol-acetate | ||
[[1bdy]] - rNPKC- | [[1bdy]] - rNPKC-δ C2 domain | ||
[[1yrk]] – hNPKC- | [[1yrk]] – hNPKC-δ C2 domain + peptide | ||
[[2yuu]] - hNPKC- | [[2yuu]] - hNPKC-δ C1 domain - NMR | ||
[[2coa]] - hNPKC- | [[2coa]] - hNPKC-δ PH domain – NMR | ||
===PKC- | ===PKC-ε=== | ||
[[1gmi]] – rNPKC- | [[1gmi]] – rNPKC-ε C2 domain | ||
===PKC- | ===PKC-τ=== | ||
[[2enj]] - hNPKC- | [[2enj]] - hNPKC-τ C2 domain – NMR | ||
[[2enn]], [[2enz]] - hNPKC- | [[2enn]], [[2enz]] - hNPKC-τ C1 domain – NMR | ||
[[1xjd]] – hNPKC- | [[1xjd]] – hNPKC-τ + saurosporine | ||
[[2jed]] - hNPKC- | [[2jed]] - hNPKC-τ kinase domain + inhibitor | ||
===PKC- | ===PKC-η=== | ||
[[2fk9]] – hNPKC- | [[2fk9]] – hNPKC-η C2 domain | ||
==Atypical PKC== | ==Atypical PKC== | ||
===PKC- | ===PKC-ι=== | ||
[[1vd2]] – hAPKC- | [[1vd2]] – hAPKC-ι PB1 domain – NMR | ||
[[1zrz]] - hAPKC- | [[1zrz]] - hAPKC-ι catalytic domain | ||
[[3a8w]], [[3a8x]] - hAPKC- | [[3a8w]], [[3a8x]] - hAPKC-ι kinase domain | ||
[[1wmh]] - hAPKC- | [[1wmh]] - hAPKC-ι PB1 domain + PAR6 alpha | ||
===PKC- | ===PKC-ν=== | ||
[[2d9z]] – hPKC- | [[2d9z]] – hPKC-ν PH domain - NMR | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 11:26, 26 October 2011
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
Conventional PKCs
PKC-a
1dsy, 3rdj – rCPKC-α C2 domain – rat
3rdl - rCPKC-α C2 domain + Pb
3gpe - rCPKC-α C2 domain + Ca + PTDINS
2eli – hCPKC-α C1 domain – human – NMR
3iw4 - hCPKC-α kinase domain + inhibitor
PKC-β
1a25 – rCPKC-β C2 domain
PKC-β2
2i0e - hCPKC-β2 catalytic domain
3pfq - rCPKC-β2 (mutant)
PKC-γ
2uzp - hCPKC-γ C2 domain
2e73 - hCPKC-γ C1 domain - NMR
1tbn, 1tbo - rCPKC-γ C2 domain – NMR
Novel PKC
PKC-δ
1ptq – mNPKC-δ C2 domain – mouse
1ptr - mNPKC-δ C2 domain + phorbol-acetate
1bdy - rNPKC-δ C2 domain
1yrk – hNPKC-δ C2 domain + peptide
2yuu - hNPKC-δ C1 domain - NMR
2coa - hNPKC-δ PH domain – NMR
PKC-ε
1gmi – rNPKC-ε C2 domain
PKC-τ
2enj - hNPKC-τ C2 domain – NMR
2enn, 2enz - hNPKC-τ C1 domain – NMR
1xjd – hNPKC-τ + saurosporine
2jed - hNPKC-τ kinase domain + inhibitor
PKC-η
2fk9 – hNPKC-η C2 domain
Atypical PKC
PKC-ι
1vd2 – hAPKC-ι PB1 domain – NMR
1zrz - hAPKC-ι catalytic domain
3a8w, 3a8x - hAPKC-ι kinase domain
1wmh - hAPKC-ι PB1 domain + PAR6 alpha
PKC-ν
2d9z – hPKC-ν PH domain - NMR
Proteopedia Page Contributors and Editors (what is this?)
Michal Harel, Alexander Berchansky, Jaime Prilusky, Joel L. Sussman