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5swf

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The structure of the PP2A B56 subunit double phosphorylated BubR1 complex

Structural highlights

5swf is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.818Å
Ligands:
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

2A5G_HUMAN The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment. The PP2A-PPP2R5C holoenzyme may specifically dephosphorylate and activate TP53 and play a role in DNA damage-induced inhibition of cell proliferation. PP2A-PPP2R5C may also regulate the ERK signaling pathway through ERK dephosphorylation.^[1] ^[2]

Publication Abstract from PubMed

Specific interactions between proteins govern essential physiological processes including signaling. Many enzymes, especially the family of serine/threonine phosphatases (PSPs: PP1, PP2A, and PP2B/calcineurin/CN), recruit substrates and regulatory proteins by binding short linear motifs (SLiMs), short sequences found within intrinsically disordered regions that mediate specific protein-protein interactions. While tremendous progress had been made in identifying where and how SLiMs bind PSPs, especially PP1 and CN, essentially nothing is known about how SLiMs bind PP2A, a validated cancer drug target. Here we describe three structures of a PP2A-SLiM interaction (B56:pS-RepoMan, B56:pS-BubR1, and B56:pSpS-BubR1), show that this PP2A-specific SLiM is defined as LSPIxE, and then use these data to discover scores of likely PP2A regulators and substrates. Together, these data provide a powerful approach not only for dissecting PP2A interaction networks in cells but also for targeting PP2A diseases, such as cancer.

Expanding the PP2A Interactome by Defining a B56-Specific SLiM.,Wang X, Bajaj R, Bollen M, Peti W, Page R Structure. 2016 Dec 6;24(12):2174-2181. doi: 10.1016/j.str.2016.09.010. Epub 2016, Oct 27. PMID:27998540^[3]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Letourneux C, Rocher G, Porteu F. B56-containing PP2A dephosphorylate ERK and their activity is controlled by the early gene IEX-1 and ERK. EMBO J. 2006 Feb 22;25(4):727-38. Epub 2006 Feb 2. PMID:16456541 doi:http://dx.doi.org/10.1038/sj.emboj.7600980
↑ Li HH, Cai X, Shouse GP, Piluso LG, Liu X. A specific PP2A regulatory subunit, B56gamma, mediates DNA damage-induced dephosphorylation of p53 at Thr55. EMBO J. 2007 Jan 24;26(2):402-11. PMID:17245430 doi:http://dx.doi.org/10.1038/sj.emboj.7601519
↑ Wang X, Bajaj R, Bollen M, Peti W, Page R. Expanding the PP2A Interactome by Defining a B56-Specific SLiM. Structure. 2016 Dec 6;24(12):2174-2181. doi: 10.1016/j.str.2016.09.010. Epub 2016, Oct 27. PMID:27998540 doi:http://dx.doi.org/10.1016/j.str.2016.09.010

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/5swf"

@@ Line 1: / Line 1: @@
 ==The structure of the PP2A B56 subunit double phosphorylated BubR1 complex==
-<StructureSection load='5swf' size='340' side='right' caption='[[5swf]], [[Resolution|resolution]] 2.82&Aring;' scene=''>
+<StructureSection load='5swf' size='340' side='right'caption='[[5swf]], [[Resolution|resolution]] 2.82&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[5swf]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5SWF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5SWF FirstGlance]. <br>
+<table><tr><td colspan='2'>[[5swf]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5SWF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5SWF FirstGlance]. <br>
-</td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.818&#8491;</td></tr>
-<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5sw9|5sw9]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></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=5swf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5swf OCA], [http://pdbe.org/5swf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5swf RCSB], [http://www.ebi.ac.uk/pdbsum/5swf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5swf ProSAT]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5swf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5swf OCA], [https://pdbe.org/5swf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5swf RCSB], [https://www.ebi.ac.uk/pdbsum/5swf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5swf ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/2A5G_HUMAN 2A5G_HUMAN]] The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment. The PP2A-PPP2R5C holoenzyme may specifically dephosphorylate and activate TP53 and play a role in DNA damage-induced inhibition of cell proliferation. PP2A-PPP2R5C may also regulate the ERK signaling pathway through ERK dephosphorylation.<ref>PMID:16456541</ref> <ref>PMID:17245430</ref>
+[https://www.uniprot.org/uniprot/2A5G_HUMAN 2A5G_HUMAN] The B regulatory subunit might modulate substrate selectivity and catalytic activity, and also might direct the localization of the catalytic enzyme to a particular subcellular compartment. The PP2A-PPP2R5C holoenzyme may specifically dephosphorylate and activate TP53 and play a role in DNA damage-induced inhibition of cell proliferation. PP2A-PPP2R5C may also regulate the ERK signaling pathway through ERK dephosphorylation.<ref>PMID:16456541</ref> <ref>PMID:17245430</ref>
 <div style="background-color:#fffaf0;">
 == Publication Abstract from PubMed ==
@@ Line 19: / Line 19: @@
 </div>
 <div class="pdbe-citations 5swf" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Protein phosphatase 3D structures|Protein phosphatase 3D structures]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: Bajaj, R]]
+[[Category: Homo sapiens]]
-[[Category: Page, R]]
+[[Category: Large Structures]]
-[[Category: Peti, W]]
+[[Category: Bajaj R]]
-[[Category: Wang, X]]
+[[Category: Page R]]
-[[Category: Cell cycle]]
+[[Category: Peti W]]
-[[Category: Hydrolase]]
+[[Category: Wang X]]
-[[Category: Phosphatase]]
-[[Category: Regulator]]
-[[Category: Slim]]

5swf

From Proteopedia

Current revision

The structure of the PP2A B56 subunit double phosphorylated BubR1 complex

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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