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'''Unreleased structure'''


The entry 6dcx is ON HOLD until Paper Publication
==iASPP-PP-1c structure and targeting of p53==
 
<StructureSection load='6dcx' size='340' side='right'caption='[[6dcx]], [[Resolution|resolution]] 3.41&Aring;' scene=''>
Authors:  
== Structural highlights ==
 
<table><tr><td colspan='2'>[[6dcx]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6DCX OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6DCX FirstGlance]. <br>
Description:  
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PPP1CA, PPP1A ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN]), PPP1R13L, IASPP, NKIP1, PPP1R13BL, RAI ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
[[Category: Unreleased Structures]]
<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>
<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=6dcx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6dcx OCA], [http://pdbe.org/6dcx PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6dcx RCSB], [http://www.ebi.ac.uk/pdbsum/6dcx PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6dcx ProSAT]</span></td></tr>
</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/IASPP_HUMAN IASPP_HUMAN]] Regulator that plays a central role in regulation of apoptosis and transcription via its interaction with NF-kappa-B and p53/TP53 proteins. Blocks transcription of HIV-1 virus by inhibiting the action of both NF-kappa-B and SP1. Also inhibits p53/TP53 function, possibly by preventing the association between p53/TP53 and ASPP1 or ASPP2, and therefore suppressing the subsequent activation of apoptosis.<ref>PMID:15489900</ref> <ref>PMID:10336463</ref> <ref>PMID:12134007</ref> <ref>PMID:12524540</ref> 
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Phosphoprotein phosphatase]]
[[Category: Edwards, R A]]
[[Category: Glover, J N.M]]
[[Category: Zhou, Y]]
[[Category: Ank repeat]]
[[Category: Aspp2]]
[[Category: Dephosphorylation]]
[[Category: Hydrolase-transcription complex]]
[[Category: Iaspp]]
[[Category: P53]]
[[Category: Pp-1c]]
[[Category: Rvxf motif]]
[[Category: Sh3]]

Revision as of 10:22, 21 May 2019

iASPP-PP-1c structure and targeting of p53iASPP-PP-1c structure and targeting of p53

Structural highlights

6dcx is a 4 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:PPP1CA, PPP1A (HUMAN), PPP1R13L, IASPP, NKIP1, PPP1R13BL, RAI (HUMAN)
Activity:Phosphoprotein phosphatase, with EC number 3.1.3.16
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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] [IASPP_HUMAN] Regulator that plays a central role in regulation of apoptosis and transcription via its interaction with NF-kappa-B and p53/TP53 proteins. Blocks transcription of HIV-1 virus by inhibiting the action of both NF-kappa-B and SP1. Also inhibits p53/TP53 function, possibly by preventing the association between p53/TP53 and ASPP1 or ASPP2, and therefore suppressing the subsequent activation of apoptosis.[2] [3] [4] [5]

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. ↑ Slee EA, Gillotin S, Bergamaschi D, Royer C, Llanos S, Ali S, Jin B, Trigiante G, Lu X. The N-terminus of a novel isoform of human iASPP is required for its cytoplasmic localization. Oncogene. 2004 Dec 2;23(56):9007-16. PMID:15489900 doi:http://dx.doi.org/1208088
  3. ↑ Yang JP, Hori M, Sanda T, Okamoto T. Identification of a novel inhibitor of nuclear factor-kappaB, RelA-associated inhibitor. J Biol Chem. 1999 May 28;274(22):15662-70. PMID:10336463
  4. ↑ Takada N, Sanda T, Okamoto H, Yang JP, Asamitsu K, Sarol L, Kimura G, Uranishi H, Tetsuka T, Okamoto T. RelA-associated inhibitor blocks transcription of human immunodeficiency virus type 1 by inhibiting NF-kappaB and Sp1 actions. J Virol. 2002 Aug;76(16):8019-30. PMID:12134007
  5. ↑ Bergamaschi D, Samuels Y, O'Neil NJ, Trigiante G, Crook T, Hsieh JK, O'Connor DJ, Zhong S, Campargue I, Tomlinson ML, Kuwabara PE, Lu X. iASPP oncoprotein is a key inhibitor of p53 conserved from worm to human. Nat Genet. 2003 Feb;33(2):162-7. Epub 2003 Jan 13. PMID:12524540 doi:http://dx.doi.org/10.1038/ng1070

6dcx, resolution 3.41Å

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