Protein kinase C
From Proteopedia
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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, phosphate 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) - 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. | '''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. | ||
Revision as of 12:19, 12 November 2012
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.
Contents |
3D structures of protein kinase C
Updated June 2012
Conventional PKCs
PKC-a
1dsy, 3rdj, 3twy – 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
4dnl - hCPKC-α C2 domain
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, Joel L. Sussman, Jaime Prilusky
