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Protein phosphatase

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<StructureSection load='' size='350' side='right' scene='54/540142/Cv/1' caption='Human PP2A catalytic (green) and regulatory (cyan) subunits complex with tumor-inducing toxin and sulfate [[3k7v]]'>
<StructureSection load='' size='350' side='right' scene='54/540142/Cv/1' caption='Human PP2A catalytic (green) and regulatory (cyan) subunits complex with tumor-inducing toxin and sulfate [[3k7v]]'>
 +
__TOC__
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== Function ==
== Function ==
'''Protein phosphatases''' (PP) or '''serine/threonine protein phosphatase''' regulate protein phosphorylation and thus are key in intracellular signal transduction processes.<br />
'''Protein phosphatases''' (PP) or '''serine/threonine protein phosphatase''' regulate protein phosphorylation and thus are key in intracellular signal transduction processes.<br />
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*<scene name='54/540142/Cv/6'>Mn+2 ion cofactors coordination site</scene>.
*<scene name='54/540142/Cv/6'>Mn+2 ion cofactors coordination site</scene>.
*<scene name='54/540142/Cv/7'>Whole binding site</scene>.
*<scene name='54/540142/Cv/7'>Whole binding site</scene>.
 +
== 3D Structures of protein phosphatase==
 +
[[Protein phosphatase 3D structures]]
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</StructureSection>
</StructureSection>
== 3D Structures of protein phosphatase==
== 3D Structures of protein phosphatase==
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**[[3n5u]] – hPP1A catalytic subunit + retinoblastoma-associated protein<br />
**[[3n5u]] – hPP1A catalytic subunit + retinoblastoma-associated protein<br />
**[[4g9j]], [[5ioh]] – hPP1A catalytic subunit + peptide<br />
**[[4g9j]], [[5ioh]] – hPP1A catalytic subunit + peptide<br />
 +
**[[6b67]] – hPP1A catalytic subunit (mutant) + peptide<br />
*Protein phosphatase 1G
*Protein phosphatase 1G
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**[[4da1]] - hPP1K + Mn<br />
**[[4da1]] - hPP1K + Mn<br />
 +
**[[6ak7]] – hPP1K (mutant) + Mg<br />
-
*Protein phosphatase 2A
+
*Protein phosphatase 2A or serine/threonine-protein phosphatase 2A
-
**[[1b3u]], [[2g62]], [[2hv6]] – hPP2A regulatory subunit <br />
+
**[[1b3u]], [[2g62]], [[2hv6]], [[4mew]], [[4i5k]], [[4i5j]], [[2jak]], [[2ixm]], [[2hv7] – hPP2A regulatory subunit <br />
 +
**[[5swf]], [[5k6s]], [[5jja]] – hPP2A regulatory subunit + BUBR1<br />
 +
**[[5sw9]] – hPP2A regulatory subunit + REPOMAN<br />
 +
**[[2pkg]], [[2pf4]] – hPP2A regulatory subunit + small T antigen<br />
**[[2ie3]], [[2ie4]], [[2npp]], [[2nyl]], [[2nym]] – hPP2A catalytic + regulatory subunit + tumor-inducing toxin<br />
**[[2ie3]], [[2ie4]], [[2npp]], [[2nyl]], [[2nym]] – hPP2A catalytic + regulatory subunit + tumor-inducing toxin<br />
**[[3c5w]] – hPP2A catalytic + regulatory subunit + PP2A-specific methyltransferase<br />
**[[3c5w]] – hPP2A catalytic + regulatory subunit + PP2A-specific methyltransferase<br />
 +
**[[3p71]], [[2iae]] – hPP2A catalytic + regulatory subunit + LCMT-1 <br />
 +
**[[3dw8]] – hPP2A catalytic + regulatory subunit (mutant) + LCMT-1 <br />
 +
**[[3fga]] – hPP2A catalytic + regulatory subunit + LCMT-1 + SGO<br />
 +
**[[4i5n]], [[4i5l]] – hPP2A catalytic + regulatory subunit + MCLR<br />
 +
**[[3k7w]] – hPP2A catalytic + regulatory subunit + toxin<br />
 +
**[[4iyp]] – hPP2A catalytic subunit + immunoglobin-binding protein<br />
 +
**[[6ef4]] – mPP2A (mutant) - mouse<br />
 +
**[[5w0w]] – mPP2A + TIPRL<br />
*Protein phosphatase 2B See [[Calcineurin]]
*Protein phosphatase 2B See [[Calcineurin]]
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**[[4raf]], [[4rag]] - hPP2C α (mutant) + Mn<br />
**[[4raf]], [[4rag]] - hPP2C α (mutant) + Mn<br />
**[[3d8k]] – PP2C – ''Toxoplasma gondii''<br />
**[[3d8k]] – PP2C – ''Toxoplasma gondii''<br />
-
**[[3jrq]], [[3nmn]] – AtPP2C + Pyl1 + pyrabactin – ''Arabidopsis thaliana''<br />
+
**[[3ujk]] – AtPP2C - ''Arabidopsis thaliana'' <br />
 +
**[[4yzg]] – AtPP2C (mutant) <br />
 +
**[[3jrq]], [[3nmn]] – AtPP2C + Pyl1 + pyrabactin <br />
**[[3kdj]] - AtPP2C + Pyl1 + abscicic acid<br />
**[[3kdj]] - AtPP2C + Pyl1 + abscicic acid<br />
**[[3nmt]], [[3kb3]], [[3nmv]], [[3ujl]] – AtPP2C + Pyl2<br />
**[[3nmt]], [[3kb3]], [[3nmv]], [[3ujl]] – AtPP2C + Pyl2<br />
**[[4la7]], [[4lg5]], [[4lga]], [[4lgb]] – AtPP2C + Pyl2 + ligand<br />
**[[4la7]], [[4lg5]], [[4lga]], [[4lgb]] – AtPP2C + Pyl2 + ligand<br />
 +
**[[5vr7]], [[5vro]], [[5vs5]], [[5vsq]], [[5vsr]], [[5vt7]] – AtPP2C + Pyl2 + quinolone derivative<br />
**[[4ds8]], [[5jo1]], [[5jo2]] – AtPP2C + Pyl3 + Mn<br />
**[[4ds8]], [[5jo1]], [[5jo2]] – AtPP2C + Pyl3 + Mn<br />
**[[3rt0]] – AtPP2C (mutant) + Pyl10<br />
**[[3rt0]] – AtPP2C (mutant) + Pyl10<br />
**[[4n0g]] – AtPP2C + Pyl13<br />
**[[4n0g]] – AtPP2C + Pyl13<br />
**[[3qn1]], [[3zvu]], [[4wvo]] – AtPP2C + Pyr1<br />
**[[3qn1]], [[3zvu]], [[4wvo]] – AtPP2C + Pyr1<br />
-
**[[3ujk]] – AtPP2C <br />
+
**[[5or2]], [[5or6]] – AtPP2C + Pyr1 + abscicic acid analog<br />
-
**[[4yzg]] – AtPP2C (mutant) <br />
+
**[[4yzh]] – AtPP2C (mutant) + chlorophyll-binding protein peptide<br />
**[[4yzh]] – AtPP2C (mutant) + chlorophyll-binding protein peptide<br />
**[[3ujg]] - AtPP2C + SRK2E<br />
**[[3ujg]] - AtPP2C + SRK2E<br />
 +
**[[5mn0]] – AtPP2C + ABA receptor <br />
*Protein phosphatase 4
*Protein phosphatase 4

Revision as of 08:36, 2 December 2019

Human PP2A catalytic (green) and regulatory (cyan) subunits complex with tumor-inducing toxin and sulfate 3k7v

Drag the structure with the mouse to rotate

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 2C
  • 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

}}

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
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