Protein kinase C

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
<StructureSection load='3gpe' size='350' side='right' caption='Rat protein kinase a C2 domain complex with phosphatidylinositol, phosphate and Ca+2 ion (green), [[3gpe]] ' scene=''>
<StructureSection load='3gpe' size='350' side='right' caption='Rat protein kinase a C2 domain complex with phosphatidylinositol, phosphate and Ca+2 ion (green), [[3gpe]] ' scene=''>
-
'''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 PKC''' (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.
+
== Function ==
 +
'''Protein kinase C''' (PKC) phosphorylates serine or threonine residues in proteins. PKC act in signal transduction pathways<ref>PMID:11440359</ref>. PKC consists of regulatory domain hinged to a catalytic domain. The regulatory domain contains the C1 region which binds diacylglycerol (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.
 +
 
 +
*'''Conventional PKC''' (CPKC) - α, β1, β2, γ – are activated by DAG, Ca+2 and a phospholipid.<br />
 +
*'''Novel PKC''' (NPKC) – δ, ε, η, θ – are activated by DAG.<br />
 +
*'''Atypical PKC''' (APKC) do not require DAG or Ca+2 for activation.
 +
 
 +
== Relevance ==
 +
Activation of PKC and elevated levels of DAG are associated with vascular abnormalities in retinal, renal and cardiovascular tissues. Inhibitors of PKC-β are tested for prevention of diabetic complications<ref>PMID:9604860</ref>. Activation of PKC-α and PKC-β are linked to malignant phenotypes while PKC-δ is thought to mediate anti-cancer effects<ref>PMID:15907369</ref>.
</StructureSection>
</StructureSection>
==3D structures of protein kinase C==
==3D structures of protein kinase C==
Line 9: Line 17:
*'''Conventional PKCs'''
*'''Conventional PKCs'''
-
*PKC-a
+
*PKC-α
**[[1dsy]], [[3rdj]], [[3twy]] – rCPKC-α C2 domain – rat
**[[1dsy]], [[3rdj]], [[3twy]] – rCPKC-α C2 domain – rat

Revision as of 09:06, 14 July 2016

Rat protein kinase a C2 domain complex with phosphatidylinositol, phosphate and Ca+2 ion (green), 3gpe

Drag the structure with the mouse to rotate

3D structures of protein kinase C

Updated on 14-July-2016

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Joel L. Sussman, Jaime Prilusky

Personal tools