This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


Protein kinase C

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 7: Line 7:
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}}
-
===Conventional PKCs===
+
==Conventional PKCs==
===PKC-a===
===PKC-a===
Line 39: Line 39:
[[1tbn]], [[1tbo]] - rCPKC-γ C2 domain – NMR
[[1tbn]], [[1tbo]] - rCPKC-γ C2 domain – NMR
-
===Novel PKC===
+
==Novel PKC==
===PKC-δ===
===PKC-δ===
Line 80: Line 80:
[[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 07:37, 20 August 2014

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

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

Proteopedia Page Contributors and Editors (what is this?)

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

Personal tools