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]] }} | |
| - | {{ | + | |
'''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. | ||
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[[3rdl]] - rCPKC-a C2 domain + Pb | [[3rdl]] - rCPKC-a C2 domain + Pb | ||
| - | [[ | + | [[3gpe]] - rCPKC-a C2 domain + Ca + PTDINS |
[[2eli]] – hCPKC-a C1 domain – human – NMR | [[2eli]] – hCPKC-a C1 domain – human – NMR | ||
Revision as of 17:26, 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
3gpe - 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
