Protein kinase C
From Proteopedia
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'''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. | ||
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==3D structures of protein kinase C== | ==3D structures of protein kinase C== | ||
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Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | ||
| - | ==Conventional PKCs== | + | ===Conventional PKCs=== |
===PKC-a=== | ===PKC-a=== | ||
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[[1tbn]], [[1tbo]] - rCPKC-γ C2 domain – NMR | [[1tbn]], [[1tbo]] - rCPKC-γ C2 domain – NMR | ||
| - | ==Novel PKC== | + | ===Novel PKC=== |
===PKC-δ=== | ===PKC-δ=== | ||
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[[4fkd]] – hNPKC-θ second Cys-rich regulatory domain<br /> | [[4fkd]] – hNPKC-θ second Cys-rich regulatory domain<br /> | ||
| - | + | ===Atypical PKC=== | |
| - | ==Atypical PKC== | + | |
===PKC-ι=== | ===PKC-ι=== | ||
Revision as of 07:36, 20 August 2014
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 on 20-August-2014
Conventional PKCs
PKC-a
1dsy, 3rdj, 3twy – rCPKC-α C2 domain – rat
3rdl, 4l1l - rCPKC-α C2 domain + ion
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
3uej - mNPKC-δ C1B domain
3uey, 3uff, 3ugd, 3ugi, 3ugl - mNPKC-δ C1B domain (mutant)
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
3txo - hNPKC-η kinase domain (mutant) + inhibitor
PKC-θ
4fkd – hNPKC-θ second Cys-rich regulatory domain
Atypical PKC
PKC-ι
1vd2 – hAPKC-ι PB1 domain – NMR
1zrz - hAPKC-ι catalytic domain
3a8w, 3a8x - hAPKC-ι kinase domain
3zh8 - hAPKC-ι kinase domain (mutant) + inhibitor
1wmh - hAPKC-ι PB1 domain + PAR6 alpha
4dc2 - hAPKC-ι residues 231-595 + PAR3 peptide
PKC-ν
2d9z – hPKC-ν PH domain - NMR
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Michal Harel, Alexander Berchansky, Joel L. Sussman, Jaime Prilusky
