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Protein phosphatase
From Proteopedia
(Difference between revisions)
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{{#tree:id=OrganizedByTopic|openlevels=0| | {{#tree:id=OrganizedByTopic|openlevels=0| | ||
| + | *Protein phosphatase 1 | ||
| + | |||
| + | **[[2rlt]] - PP1 regulatory subunit - pig - NMR<br /> | ||
| + | |||
*Protein phosphatase 1A | *Protein phosphatase 1A | ||
**[[3fxj]], [[3fxk]], [[3fxl]], [[3fxm]], [[3fxo]], [[4ra2]] – hPP1A + Mn – human<br /> | **[[3fxj]], [[3fxk]], [[3fxl]], [[3fxm]], [[3fxo]], [[4ra2]] – hPP1A + Mn – human<br /> | ||
| - | **[[4da1]] – hPP1K + Mn<br /> | ||
**[[3n5u]] – hPP1A catalytic subunit + retinoblastoma-associated protein<br /> | **[[3n5u]] – hPP1A catalytic subunit + retinoblastoma-associated protein<br /> | ||
| - | **[[3v4y]] – hPP1A catalytic subunit + PP1 nuclear inhibitor<br /> | ||
**[[4g9j]], [[5ioh]] – hPP1A catalytic subunit + peptide<br /> | **[[4g9j]], [[5ioh]] – hPP1A catalytic subunit + peptide<br /> | ||
| + | |||
| + | *Protein phosphatase 1G | ||
| + | |||
**[[5inb]], [[5j28]] - hPP1G catalytic subunit + peptide<br /> | **[[5inb]], [[5j28]] - hPP1G catalytic subunit + peptide<br /> | ||
| - | **[[ | + | |
| + | *Protein phosphatase 1K | ||
| + | |||
| + | **[[4da1]] - hPP1K + Mn<br /> | ||
*Protein phosphatase 2A | *Protein phosphatase 2A | ||
| Line 40: | Line 48: | ||
**[[2iq1]] – hPP2C κ <br /> | **[[2iq1]] – hPP2C κ <br /> | ||
| + | **[[4raf]], [[4rag]] - hPP2C α (mutant) + Mn<br /> | ||
**[[3d8k]] – PP2C – ''Toxoplasma gondii''<br /> | **[[3d8k]] – PP2C – ''Toxoplasma gondii''<br /> | ||
| - | **[[3jrq]], [[3nmn]] – AtPP2C + Pyl1 – ''Arabidopsis thaliana''<br /> | + | **[[3jrq]], [[3nmn]] – AtPP2C + Pyl1 + pyrabactin – ''Arabidopsis thaliana''<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 /> | ||
| - | **[[4ds8]] – 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 /> | ||
| Line 51: | Line 61: | ||
**[[4yzg]] – AtPP2C (mutant) <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 /> | |
}} | }} | ||
== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | [[Category:Topic Page]] | ||
Revision as of 18:26, 21 September 2017
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3D Structures of protein phosphatase
Updated on 21-September-2017
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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