Protein phosphatase

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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 Contents 1 Function 2 Disease 3 Structural highlights 4 3D Structures of protein phosphatase 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[1]. PP2A targets proteins in the oncogenic signaling pathways[2]. 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[3]. PP5 is activated by lipids and is involved in signal transduction[4]. Disease Mutations in PP2A are found in many solid cancers and leukemias. PP2A-activating drugs are possible candidates for cancer therapeutics protocols[5]. Development of Alzheimer disease drugs could be based on restoration of PP2A activity[6]. Structural highlights . Algal toxin binds at the surface pocket of the PP2A catalytic subunit which contains the Mn+2 ion cofactors[7]. Water molecule are shown as red sphere. . . 3D Structures of protein phosphatase Protein phosphatase 3D structures

3D Structures of protein phosphatase

Updated on 02-December-2019 {{#tree:id=OrganizedByTopic|openlevels=0|

• Protein phosphatase 1

• • 2rlt - PP1 regulatory subunit - pig - NMR
    

• Protein phosphatase 1A

• • 3fxj, 3fxk, 3fxl, 3fxm, 3fxo, 4ra2 – hPP1A + Mn – human
    
  • 3n5u – hPP1A catalytic subunit + retinoblastoma-associated protein
    
  • 4g9j, 5ioh – hPP1A catalytic subunit + peptide
    
  • 6b67 – hPP1A catalytic subunit (mutant) + peptide
    

• Protein phosphatase 1G

• • 5inb, 5j28 - hPP1G catalytic subunit + peptide
    

• Protein phosphatase 1K

• • 4da1 - hPP1K + Mn
    
  • 6ak7 – hPP1K (mutant) + Mg
    

• Protein phosphatase 2A or serine/threonine-protein phosphatase 2A

• • 1b3u, 2g62, 2hv6, 4mew, 4i5k, 4i5j, 2jak, 2ixm, [[2hv7] – hPP2A regulatory subunit
    
  • 5swf, 5k6s, 5jja – hPP2A regulatory subunit + BUBR1
    
  • 5sw9 – hPP2A regulatory subunit + REPOMAN
    
  • 2pkg, 2pf4 – hPP2A regulatory subunit + small T antigen
    
  • 2ie3, 2ie4, 2npp, 2nyl, 2nym – hPP2A catalytic + regulatory subunit + tumor-inducing toxin
    
  • 3c5w – hPP2A catalytic + regulatory subunit + PP2A-specific methyltransferase
    
  • 3p71, 2iae – hPP2A catalytic + regulatory subunit + LCMT-1
    
  • 3dw8 – hPP2A catalytic + regulatory subunit (mutant) + LCMT-1
    
  • 3fga – hPP2A catalytic + regulatory subunit + LCMT-1 + SGO
    
  • 4i5n, 4i5l – hPP2A catalytic + regulatory subunit + MCLR
    
  • 3k7w – hPP2A catalytic + regulatory subunit + toxin
    
  • 4iyp – hPP2A catalytic subunit + immunoglobin-binding protein
    
  • 6ef4 – mPP2A (mutant) - mouse
    
  • 5w0w – mPP2A + TIPRL
    

• Protein phosphatase 2B See Calcineurin

• Protein phosphatase 2C

• • 2iq1 – hPP2C κ
    
  • 4raf, 4rag - hPP2C α (mutant) + Mn
    
  • 3d8k – PP2C – Toxoplasma gondii
    
  • 3ujk – AtPP2C - Arabidopsis thaliana
    
  • 4yzg – AtPP2C (mutant)
    
  • 3jrq, 3nmn – AtPP2C + Pyl1 + pyrabactin
    
  • 3kdj - AtPP2C + Pyl1 + abscicic acid
    
  • 3nmt, 3kb3, 3nmv, 3ujl – AtPP2C + Pyl2
    
  • 4la7, 4lg5, 4lga, 4lgb – AtPP2C + Pyl2 + ligand
    
  • 5vr7, 5vro, 5vs5, 5vsq, 5vsr, 5vt7 – AtPP2C + Pyl2 + quinolone derivative
    
  • 4ds8, 5jo1, 5jo2 – AtPP2C + Pyl3 + Mn
    
  • 3rt0 – AtPP2C (mutant) + Pyl10
    
  • 4n0g – AtPP2C + Pyl13
    
  • 3qn1, 3zvu, 4wvo – AtPP2C + Pyr1
    
  • 5or2, 5or6 – AtPP2C + Pyr1 + abscicic acid analog
    
  • 4yzh – AtPP2C (mutant) + chlorophyll-binding protein peptide
    
  • 3ujg - AtPP2C + SRK2E
    
  • 5mn0 – AtPP2C + ABA receptor
    

• 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
    

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References

1. ↑ Ragolia L, Begum N. Protein phosphatase-1 and insulin action. Mol Cell Biochem. 1998 May;182(1-2):49-58. PMID:9609113
2. ↑ Resjo S, Goransson O, Harndahl L, Zolnierowicz S, Manganiello V, Degerman E. Protein phosphatase 2A is the main phosphatase involved in the regulation of protein kinase B in rat adipocytes. Cell Signal. 2002 Mar;14(3):231-8. PMID:11812651
3. ↑ Lipinszki Z, Lefevre S, Savoian MS, Singleton MR, Glover DM, Przewloka MR. Centromeric binding and activity of Protein Phosphatase 4. Nat Commun. 2015 Jan 6;6:5894. doi: 10.1038/ncomms6894. PMID:25562660 doi:http://dx.doi.org/10.1038/ncomms6894
4. ↑ Chinkers M. Protein phosphatase 5 in signal transduction. Trends Endocrinol Metab. 2001 Jan-Feb;12(1):28-32. PMID:11137038
5. ↑ Perrotti D, Neviani P. Protein phosphatase 2A: a target for anticancer therapy. Lancet Oncol. 2013 May;14(6):e229-38. doi: 10.1016/S1470-2045(12)70558-2. PMID:23639323 doi:http://dx.doi.org/10.1016/S1470-2045(12)70558-2
6. ↑ Rudrabhatla P, Pant HC. Role of protein phosphatase 2A in Alzheimer's disease. Curr Alzheimer Res. 2011 Sep;8(6):623-32. PMID:21605044
7. ↑ Huhn J, Jeffrey PD, Larsen K, Rundberget T, Rise F, Cox NR, Arcus V, Shi Y, Miles CO. A structural basis for the reduced toxicity of dinophysistoxin-2. Chem Res Toxicol. 2009 Nov;22(11):1782-6. PMID:19916524 doi:10.1021/tx9001622