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'''Unreleased structure'''
==Crystal Structure of Protein Phosphate 1 complexed with PP1 binding domain of GADD34==
 
<StructureSection load='4xpn' size='340' side='right' caption='[[4xpn]], [[Resolution|resolution]] 2.29&Aring;' scene=''>
The entry 4xpn is ON HOLD  until Paper Publication
== Structural highlights ==
 
<table><tr><td colspan='2'>[[4xpn]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4XPN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4XPN FirstGlance]. <br>
Authors: Choy, M.S., Peti, W., Page, R.
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
 
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Phosphoprotein_phosphatase Phosphoprotein phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.16 3.1.3.16] </span></td></tr>
Description:  
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4xpn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4xpn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4xpn RCSB], [http://www.ebi.ac.uk/pdbsum/4xpn PDBsum]</span></td></tr>
[[Category: Unreleased Structures]]
</table>
== Function ==
[[http://www.uniprot.org/uniprot/PP1A_HUMAN PP1A_HUMAN]] Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase 1 (PP1) is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in dephosphorylating substrates such as the postsynaptic density-associated Ca(2+)/calmodulin dependent protein kinase II. Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. Regulates NEK2 function in terms of kinase activity and centrosome number and splitting, both in the presence and absence of radiation-induced DNA damage. Regulator of neural tube and optic fissure closure, and enteric neural crest cell (ENCCs) migration during development.<ref>PMID:17283141</ref>  [[http://www.uniprot.org/uniprot/PR15A_HUMAN PR15A_HUMAN]] Recruits the serine/threonine-protein phosphatase PP1 to dephosphorylate the translation initiation factor eIF-2A/EIF2S1, thereby reversing the shut-off of protein synthesis initiated by stress-inducible kinases and facilitating recovery of cells from stress. Down-regulates the TGF-beta signaling pathway by promoting dephosphorylation of TGFB1 by PP1. May promote apoptosis by inducing TP53 phosphorylation on 'Ser-15'.<ref>PMID:11564868</ref> <ref>PMID:12556489</ref> <ref>PMID:14635196</ref> <ref>PMID:14718519</ref> <ref>PMID:8139541</ref> 
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Phosphoprotein phosphatase]]
[[Category: Choy, M S]]
[[Category: Page, R]]
[[Category: Page, R]]
[[Category: Choy, M.S]]
[[Category: Peti, W]]
[[Category: Peti, W]]
[[Category: Eif2alpha phosphatase]]
[[Category: Hydrolase]]
[[Category: Pp1 regulator]]

Revision as of 15:23, 1 July 2015

Crystal Structure of Protein Phosphate 1 complexed with PP1 binding domain of GADD34Crystal Structure of Protein Phosphate 1 complexed with PP1 binding domain of GADD34

Structural highlights

4xpn is a 4 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:, ,
Activity:Phosphoprotein phosphatase, with EC number 3.1.3.16
Resources:FirstGlance, OCA, RCSB, PDBsum

Function

[PP1A_HUMAN] Protein phosphatase that associates with over 200 regulatory proteins to form highly specific holoenzymes which dephosphorylate hundreds of biological targets. Protein phosphatase 1 (PP1) is essential for cell division, and participates in the regulation of glycogen metabolism, muscle contractility and protein synthesis. Involved in regulation of ionic conductances and long-term synaptic plasticity. May play an important role in dephosphorylating substrates such as the postsynaptic density-associated Ca(2+)/calmodulin dependent protein kinase II. Component of the PTW/PP1 phosphatase complex, which plays a role in the control of chromatin structure and cell cycle progression during the transition from mitosis into interphase. Regulates NEK2 function in terms of kinase activity and centrosome number and splitting, both in the presence and absence of radiation-induced DNA damage. Regulator of neural tube and optic fissure closure, and enteric neural crest cell (ENCCs) migration during development.[1] [PR15A_HUMAN] Recruits the serine/threonine-protein phosphatase PP1 to dephosphorylate the translation initiation factor eIF-2A/EIF2S1, thereby reversing the shut-off of protein synthesis initiated by stress-inducible kinases and facilitating recovery of cells from stress. Down-regulates the TGF-beta signaling pathway by promoting dephosphorylation of TGFB1 by PP1. May promote apoptosis by inducing TP53 phosphorylation on 'Ser-15'.[2] [3] [4] [5] [6]

References

  1. ↑ Mi J, Guo C, Brautigan DL, Larner JM. Protein phosphatase-1alpha regulates centrosome splitting through Nek2. Cancer Res. 2007 Feb 1;67(3):1082-9. PMID:17283141 doi:10.1158/0008-5472.CAN-06-3071
  2. ↑ Connor JH, Weiser DC, Li S, Hallenbeck JM, Shenolikar S. Growth arrest and DNA damage-inducible protein GADD34 assembles a novel signaling complex containing protein phosphatase 1 and inhibitor 1. Mol Cell Biol. 2001 Oct;21(20):6841-50. PMID:11564868 doi:http://dx.doi.org/10.1128/MCB.21.20.6841-6850.2001
  3. ↑ Brush MH, Weiser DC, Shenolikar S. Growth arrest and DNA damage-inducible protein GADD34 targets protein phosphatase 1 alpha to the endoplasmic reticulum and promotes dephosphorylation of the alpha subunit of eukaryotic translation initiation factor 2. Mol Cell Biol. 2003 Feb;23(4):1292-303. PMID:12556489
  4. ↑ Yagi A, Hasegawa Y, Xiao H, Haneda M, Kojima E, Nishikimi A, Hasegawa T, Shimokata K, Isobe K. GADD34 induces p53 phosphorylation and p21/WAF1 transcription. J Cell Biochem. 2003 Dec 15;90(6):1242-9. PMID:14635196 doi:http://dx.doi.org/10.1002/jcb.10711
  5. ↑ Shi W, Sun C, He B, Xiong W, Shi X, Yao D, Cao X. GADD34-PP1c recruited by Smad7 dephosphorylates TGFbeta type I receptor. J Cell Biol. 2004 Jan 19;164(2):291-300. Epub 2004 Jan 12. PMID:14718519 doi:10.1083/jcb.200307151
  6. ↑ Zhan Q, Lord KA, Alamo I Jr, Hollander MC, Carrier F, Ron D, Kohn KW, Hoffman B, Liebermann DA, Fornace AJ Jr. The gadd and MyD genes define a novel set of mammalian genes encoding acidic proteins that synergistically suppress cell growth. Mol Cell Biol. 1994 Apr;14(4):2361-71. PMID:8139541

4xpn, resolution 2.29Å

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