Protein phosphatase

spinqualitylabelsall models Human PP2A catalytic (green) and regulatory (cyan) subunits complex with tumor-inducing toxin and sulfate 3k7v Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Function Protein phosphatases (PP) or serine/threonine protein phosphatase regulate protein phosphorylation and thus are key in intracellular signal transduction processes. PP1 is a serine/threonine phosphatase and is a key component of the insulin signaling pathway. PP2A targets proteins in the oncogenic signaling pathways. For PP2A see also HEAT Repeat. PP2C are Mg/Mn-dependent and are essential for the regulation of cell cycle and stress signaling pathways. For details see ABA-regulated Protein Phosphatase 2C and ABA Signaling Pathway. PP4 regulates a variety of cellular functions. PP5 is activated by lipids and is involved in signal transduction. Disease Mutations in PP2A are found in many solid cancers and leukemias. PP2A-activating drugs are possible candidates for cancer therapeutics protocols. Development of Alzheimer disease drugs could be based on restoration of PP2A activity. Structural highlights Human PP2A catalytic (green) and regulatory (cyan) subunits complex with tumor-inducing toxin. Algal toxin binds at the surface pocket of the PP2A catalytic subunit which contains the Mn+2 ion cofactors. Water molecule are shown as red sphere. Mn+2 ion cofactors coordination site. Whole binding site.

3D Structures of protein phosphatase

Updated on 18-August-2019

{"openlevels":0}

• Protein phosphatase 1
  • HEAT Repeat - PP1 regulatory subunit - pig - NMR
    
• Protein phosphatase 1A
  • ABA-regulated Protein Phosphatase 2C, ABA Signaling Pathway, 3fxl, 3fxm, 3fxo, 4ra2 – hPP1A + Mn – human
    
  • 3n5u – hPP1A catalytic subunit + retinoblastoma-associated protein
    
  • 4g9j, 5ioh – hPP1A catalytic subunit + peptide
    
• Protein phosphatase 1G
  • 5inb, 5j28 - hPP1G catalytic subunit + peptide
    
• Protein phosphatase 1K
  • 4da1 - hPP1K + Mn
    
• Protein phosphatase 2A
  • 1b3u, 2g62, 2hv6 – hPP2A regulatory subunit
    
  • 2ie3, 2ie4, 2npp, 2nyl, 2nym – hPP2A catalytic + regulatory subunit + tumor-inducing toxin
    
  • 3c5w – hPP2A catalytic + regulatory subunit + PP2A-specific methyltransferase
    
• Protein phosphatase 2B See Calcineurin
• Protein phosphatase 2C
  • 2iq1 – hPP2C κ
    
  • 4raf, 4rag - hPP2C α (mutant) + Mn
    
  • 3d8k – PP2C – Toxoplasma gondii
    
  • 3jrq, 3nmn – AtPP2C + Pyl1 + pyrabactin – Arabidopsis thaliana
    
  • 3kdj - AtPP2C + Pyl1 + abscicic acid
    
  • 3nmt, 3kb3, 3nmv, 3ujl – AtPP2C + Pyl2
    
  • 4la7, 4lg5, 4lga, 4lgb – AtPP2C + Pyl2 + ligand
    
  • 4ds8, 5jo1, 5jo2 – AtPP2C + Pyl3 + Mn
    
  • 3rt0 – AtPP2C (mutant) + Pyl10
    
  • 4n0g – AtPP2C + Pyl13
    
  • 3qn1, 3zvu, 4wvo – AtPP2C + Pyr1
    
  • 3ujk – AtPP2C
    
  • 4yzg – AtPP2C (mutant)
    
  • 4yzh – AtPP2C (mutant) + chlorophyll-binding protein peptide
    
  • 3ujg - AtPP2C + SRK2E
    
• Protein phosphatase 4
  • 4wsf – PP4 regulatory subunit + Cenp-C – Drosophila melanogaster
    
• Protein phosphatase 5
  • 1wao – hPP5 + Mn
    
  • 5muf – hPP5
    
  • 1a17 – hPP5 protein-interacting domain
    
  • 2bug – hPP5 protein-interacting domain (mutant) + Hsp90 peptide - NMR
    
  • 1s95, 3h60 – hPP5 catalytic domain + Mn
    
  • 3h61, 3h62, 3h63, 3h64, 3h66, 3h67, 3h68, 3h69, 4zvz, 4zx2, 4zvz, 4zx2 – hPP5 catalytic domain + inhibitor + Mn
    
  • 5hpe – hPP5 catalytic domain/Hsp90 peptide + Mn
    
  • 4ja7, 4ja9 - rPP5 catalytic domain + inhibitor
    
  • 3icf - yPP5 catalytic domain + Fe - yeast
    
  • 5jjt – AtPP5 + Ni
    
• Protein phosphatase
  • 1g5b – PP + Mn – Enterobacteria phage λ
    
  • 2pk0 – PP + Mg – Streptococcus agalactiae
    
  • 2cm1 – PP + Mn – Mycobacterium tuberculosis
    
  • 3pu9 – PP + Mg – Sphaerobacter thermophilus
    
  • 5f1m – PP Stp1 + Mn – Staphylococcus aureus
    
  • 5jpf – PP Z1 + microcystin-LR + Mn – Candida albicans
    

Proteopedia Page Contributors and Editors (what is this?)

Michal Harel, Alexander Berchansky, Alexsandra Tifane Santos do Nascimento, Joel L. Sussman