Protein phosphatase
From Proteopedia
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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]]'> | ||
== Function == | == Function == | ||
| - | '''Protein phosphatases''' (PP) 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 /> |
* '''PP1''' is a serine/threonine phosphatase and is a key component of the insulin signaling pathway<ref>PMID:9609113</ref>.<br /> | * '''PP1''' is a serine/threonine phosphatase and is a key component of the insulin signaling pathway<ref>PMID:9609113</ref>.<br /> | ||
* '''PP2A''' targets proteins in the oncogenic signaling pathways<ref>PMID:11812651</ref>. For PP2A see also [[HEAT Repeat]].<br /> | * '''PP2A''' targets proteins in the oncogenic signaling pathways<ref>PMID:11812651</ref>. For PP2A see also [[HEAT Repeat]].<br /> | ||
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**[[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 /> | ||
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| + | *Protein phosphatase 2B See [[Calcineurin]] | ||
*Protein phosphatase 2C | *Protein phosphatase 2C | ||
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**[[4yzh]] – AtPP2C (mutant) + chlorophyll-binding protein peptide<br /> | **[[4yzh]] – AtPP2C (mutant) + chlorophyll-binding protein peptide<br /> | ||
**[[3ujg]] - AtPP2C + SRK2E<br /> | **[[3ujg]] - AtPP2C + SRK2E<br /> | ||
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| + | *Protein phosphatase 4 | ||
| + | |||
| + | **[[4wsf]] – PP4 regulatory subunit + Cenp-C – ''Drosophila melanogaster''<br /> | ||
| + | |||
| + | *Protein phosphatase 5 | ||
| + | |||
| + | **[[1wao]] – hPP5 + Mn<br /> | ||
| + | **[[5muf]] – hPP5 <br /> | ||
| + | **[[1a17]] – hPP5 protein-interacting domain<br /> | ||
| + | **[[2bug]] – hPP5 protein-interacting domain (mutant) + Hsp90 peptide - NMR<br /> | ||
| + | **[[1s95]], [[3h60]] – hPP5 catalytic domain + Mn<br /> | ||
| + | **[[3h61]], [[3h62]], [[3h63]], [[3h64]], [[3h66]], [[3h67]], [[3h68]], [[3h69]], [[4zvz]], [[4zx2]], [[4zvz]], [[4zx2]] – hPP5 catalytic domain + inhibitor + Mn<br /> | ||
| + | **[[5hpe]] – hPP5 catalytic domain/Hsp90 peptide + Mn<br /> | ||
| + | **[[4ja7]], [[4ja9]] - rPP5 catalytic domain + inhibitor <br /> | ||
| + | **[[3icf]] - yPP5 catalytic domain + Fe - yeast<br /> | ||
| + | **[[5jjt]] – AtPP5 + Ni<br /> | ||
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| + | *Protein phosphatase | ||
| + | |||
| + | **[[1g5b]] – PP + Mn – Enterobacteria phage λ<br /> | ||
| + | **[[2pk0]] – PP + Mg – ''Streptococcus agalactiae''<br /> | ||
| + | **[[2cm1]] – PP + Mn – ''Mycobacterium tuberculosis''<br /> | ||
| + | **[[3pu9]] – PP + Mg – ''Sphaerobacter thermophilus''<br /> | ||
| + | **[[5f1m]] – PP Stp1 + Mn – ''Staphylococcus aureus''<br /> | ||
| + | **[[5jpf]] – PP Z1 + microcystin-LR + Mn – ''Candida albicans''<br /> | ||
}} | }} | ||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 21:50, 18 September 2018
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3D Structures of protein phosphatase
Updated on 18-September-2018
References
- ↑ Ragolia L, Begum N. Protein phosphatase-1 and insulin action. Mol Cell Biochem. 1998 May;182(1-2):49-58. PMID:9609113
- ↑ 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
- ↑ 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
- ↑ Chinkers M. Protein phosphatase 5 in signal transduction. Trends Endocrinol Metab. 2001 Jan-Feb;12(1):28-32. PMID:11137038
- ↑ 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
- ↑ Rudrabhatla P, Pant HC. Role of protein phosphatase 2A in Alzheimer's disease. Curr Alzheimer Res. 2011 Sep;8(6):623-32. PMID:21605044
- ↑ 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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