Protein kinase C

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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]] }}
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'''Protein kinase C''' (PKC) phosphorylate serine or threonine residues in proteins. They act in signal transduction pathways. Conventional PKC (CPKC) - a, b1, b2, g – are activated by diacylglycerol (DAG), Ca+2 and a phospholipid. Novel PKC (NPKC) – d, e, eta, theta – 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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'''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===
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[[1dsy]], [[3rdj]] – rCPKC-a C2 domain – rat
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[[1dsy]], [[3rdj]] – rCPKC-α C2 domain – rat
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[[3rdl]] - rCPKC-a C2 domain + Pb
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[[3rdl]] - rCPKC-α C2 domain + Pb
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[[3gpe]] - rCPKC-a C2 domain + Ca + PTDINS
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[[3gpe]] - rCPKC-α C2 domain + Ca + PTDINS
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[[2eli]] – hCPKC-a C1 domain – human – NMR
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[[2eli]] – hCPKC-α C1 domain – human – NMR
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[[3iw4]] - hCPKC-a kinase domain + inhibitor
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[[3iw4]] - hCPKC-α kinase domain + inhibitor
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===PKC-b===
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===PKC-β===
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[[1a25]] – rCPKC-b C2 domain
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[[1a25]] – rCPKC-β C2 domain
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===PKC-b2===
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===PKC-β2===
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[[2i0e]] - hCPKC-b2 catalytic domain
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[[2i0e]] - hCPKC-β2 catalytic domain
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[[3pfq]] - rCPKC-b2 (mutant)
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[[3pfq]] - rCPKC-β2 (mutant)
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===PKC-g===
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===PKC-γ===
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[[2uzp]] - hCPKC-g C2 domain
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[[2uzp]] - hCPKC-γ C2 domain
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[[2e73]] - hCPKC-g C1 domain - NMR
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[[2e73]] - hCPKC-γ C1 domain - NMR
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[[1tbn]], [[1tbo]] - rCPKC-g C2 domain – NMR
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[[1tbn]], [[1tbo]] - rCPKC-γ C2 domain – NMR
==Novel PKC==
==Novel PKC==
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===PKC-d===
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===PKC-δ===
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[[1ptq]] – mNPKC-d C2 domain – mouse
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[[1ptq]] – mNPKC-δ C2 domain – mouse
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[[1ptr]] - mNPKC-d C2 domain + phorbol-acetate
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[[1ptr]] - mNPKC-δ C2 domain + phorbol-acetate
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[[1bdy]] - rNPKC-d C2 domain
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[[1bdy]] - rNPKC-δ C2 domain
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[[1yrk]] – hNPKC-d C2 domain + peptide
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[[1yrk]] – hNPKC-δ C2 domain + peptide
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[[2yuu]] - hNPKC-d C1 domain - NMR
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[[2yuu]] - hNPKC-δ C1 domain - NMR
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[[2coa]] - hNPKC-d PH domain – NMR
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[[2coa]] - hNPKC-δ PH domain – NMR
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===PKC-e===
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===PKC-ε===
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[[1gmi]] – rNPKC-e C2 domain
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[[1gmi]] – rNPKC-ε C2 domain
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===PKC-t===
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===PKC-τ===
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[[2enj]] - hNPKC-t C2 domain – NMR
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[[2enj]] - hNPKC-τ C2 domain – NMR
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[[2enn]], [[2enz]] - hNPKC-t C1 domain – NMR
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[[2enn]], [[2enz]] - hNPKC-τ C1 domain – NMR
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[[1xjd]] – hNPKC-t + saurosporine
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[[1xjd]] – hNPKC-τ + saurosporine
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[[2jed]] - hNPKC-t kinase domain + inhibitor
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[[2jed]] - hNPKC-τ kinase domain + inhibitor
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===PKC-eta===
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===PKC-η===
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[[2fk9]] – hNPKC-eta C2 domain
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[[2fk9]] – hNPKC-η C2 domain
==Atypical PKC==
==Atypical PKC==
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===PKC-i===
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===PKC-ι===
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[[1vd2]] – hAPKC-i PB1 domain – NMR
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[[1vd2]] – hAPKC-ι PB1 domain – NMR
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[[1zrz]] - hAPKC-i catalytic domain
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[[1zrz]] - hAPKC-ι catalytic domain
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[[3a8w]], [[3a8x]] - hAPKC-i kinase domain
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[[3a8w]], [[3a8x]] - hAPKC-ι kinase domain
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[[1wmh]] - hAPKC-i PB1 domain + PAR6 alpha
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[[1wmh]] - hAPKC-ι PB1 domain + PAR6 alpha
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===PKC-nu===
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===PKC-ν===
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[[2d9z]] – hPKC-nu PH domain - NMR
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[[2d9z]] – hPKC-ν PH domain - NMR
[[Category:Topic Page]]
[[Category:Topic Page]]

Revision as of 11:26, 26 October 2011

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.

Contents

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, Joel L. Sussman, Jaime Prilusky

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