Protein kinase C
From Proteopedia
(New page: '''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 ...) |
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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. | '''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. | ||
==3D structures of protein kinase C== | ==3D structures of protein kinase C== | ||
| - | ==Conventional | + | ==Conventional PKCs== |
| - | === | + | ===PKC-a=== |
[[1dsy]], [[3rdj]] – rCPKC-a C2 domain – rat | [[1dsy]], [[3rdj]] – rCPKC-a C2 domain – rat | ||
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[[3iw4]] - hCPKC-a kinase domain + inhibitor | [[3iw4]] - hCPKC-a kinase domain + inhibitor | ||
| - | === | + | ===PKC-b=== |
[[1a25]] – rCPKC-b C2 domain | [[1a25]] – rCPKC-b C2 domain | ||
| - | === | + | ===PKC-b2=== |
[[2i0e]] - hCPKC-b2 catalytic domain | [[2i0e]] - hCPKC-b2 catalytic domain | ||
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[[3pfq]] - rCPKC-b2 (mutant) | [[3pfq]] - rCPKC-b2 (mutant) | ||
| - | === | + | ===PKC-g=== |
[[2uzp]] - hCPKC-g C2 domain | [[2uzp]] - hCPKC-g C2 domain | ||
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==Novel PKC== | ==Novel PKC== | ||
| - | === | + | ===PKC-d=== |
[[1ptq]] – mNPKC-d C2 domain – mouse | [[1ptq]] – mNPKC-d C2 domain – mouse | ||
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[[2coa]] - hNPKC-d PH domain – NMR | [[2coa]] - hNPKC-d PH domain – NMR | ||
| - | === | + | ===PKC-e=== |
| - | 1gmi]] – rNPKC-e C2 domain | + | [[1gmi]] – rNPKC-e C2 domain |
| - | === | + | ===PKC-t=== |
[[2enj]] - hNPKC-t C2 domain – NMR | [[2enj]] - hNPKC-t C2 domain – NMR | ||
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[[2jed]] - hNPKC-t kinase domain + inhibitor | [[2jed]] - hNPKC-t kinase domain + inhibitor | ||
| - | === | + | ===PKC-eta=== |
[[2fk9]] – hNPKC-eta C2 domain | [[2fk9]] – hNPKC-eta C2 domain | ||
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==Atypical PKC== | ==Atypical PKC== | ||
| - | === | + | ===PKC-i=== |
[[1vd2]] – hAPKC-i PB1 domain – NMR | [[1vd2]] – hAPKC-i PB1 domain – NMR | ||
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[[1wmh]] - hAPKC-i PB1 domain + PAR6 alpha | [[1wmh]] - hAPKC-i PB1 domain + PAR6 alpha | ||
| - | === | + | ===PKC-nu=== |
[[2d9z]] – hPKC-nu PH domain - NMR | [[2d9z]] – hPKC-nu PH domain - NMR | ||
Revision as of 17:08, 12 October 2011
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.
Contents |
3D structures of protein kinase C
Conventional PKCs
PKC-a
1dsy, 3rdj – rCPKC-a C2 domain – rat
3rdl - rCPKC-a C2 domain + Pb
3pge - rCPKC-a C2 domain + Ca + PTDINS
2eli – hCPKC-a C1 domain – human – NMR
3iw4 - hCPKC-a kinase domain + inhibitor
PKC-b
1a25 – rCPKC-b C2 domain
PKC-b2
2i0e - hCPKC-b2 catalytic domain
3pfq - rCPKC-b2 (mutant)
PKC-g
2uzp - hCPKC-g C2 domain
2e73 - hCPKC-g C1 domain - NMR
1tbn, 1tbo - rCPKC-g C2 domain – NMR
Novel PKC
PKC-d
1ptq – mNPKC-d C2 domain – mouse
1ptr - mNPKC-d C2 domain + phorbol-acetate
1bdy - rNPKC-d C2 domain
1yrk – hNPKC-d C2 domain + peptide
2yuu - hNPKC-d C1 domain - NMR
2coa - hNPKC-d PH domain – NMR
PKC-e
1gmi – rNPKC-e C2 domain
PKC-t
2enj - hNPKC-t C2 domain – NMR
2enn, 2enz - hNPKC-t C1 domain – NMR
1xjd – hNPKC-t + saurosporine
2jed - hNPKC-t kinase domain + inhibitor
PKC-eta
2fk9 – hNPKC-eta C2 domain
Atypical PKC
PKC-i
1vd2 – hAPKC-i PB1 domain – NMR
1zrz - hAPKC-i catalytic domain
3a8w, 3a8x - hAPKC-i kinase domain
1wmh - hAPKC-i PB1 domain + PAR6 alpha
PKC-nu
2d9z – hPKC-nu PH domain - NMR
Proteopedia Page Contributors and Editors (what is this?)
Michal Harel, Alexander Berchansky, Joel L. Sussman, Jaime Prilusky
