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[[Image:2jak.gif|left|200px]]


<!--
==Human PP2A regulatory subunit B56g==
The line below this paragraph, containing "STRUCTURE_2jak", creates the "Structure Box" on the page.
<StructureSection load='2jak' size='340' side='right'caption='[[2jak]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[2jak]] is a 1 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=2JAK OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JAK FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</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=2jak FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jak OCA], [https://pdbe.org/2jak PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jak RCSB], [https://www.ebi.ac.uk/pdbsum/2jak PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jak ProSAT]</span></td></tr>
{{STRUCTURE_2jak|  PDB=2jak  |  SCENE=  }}
</table>
== Function ==
[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>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ja/2jak_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2jak ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The PP2A serine/threonine phosphatase regulates a plethora of cellular processes. In the cell the predominant form of the enzyme is a heterotrimer, formed by a core dimer composed of a catalytic and a scaffolding subunit, which assemble together with one of a range of different regulatory B subunits. Here, we present the first structure of a free non-complexed B subunit, B56 gamma. Comparison with the recent structures of a heterotrimeric complex and the core dimer reveals several significant conformational changes in the interface region between the B56 gamma and the core dimer. These allow for an assembly scheme of the PP2A holoenzyme to be put forth where B56 gamma first complexes with the scaffolding subunit and subsequently binds to the catalytic subunit and this induces the formation of a binding site for the invariant C-terminus of the catalytic subunit that locks in the complex as a last step of assembly.


'''HUMAN PP2A REGULATORY SUBUNIT B56G'''
The structure of the PP2A regulatory subunit B56 gamma: the remaining piece of the PP2A jigsaw puzzle.,Magnusdottir A, Stenmark P, Flodin S, Nyman T, Kotenyova T, Graslund S, Ogg D, Nordlund P Proteins. 2009 Jan;74(1):212-21. PMID:18618707<ref>PMID:18618707</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2jak" style="background-color:#fffaf0;"></div>


==About this Structure==
==See Also==
2JAK is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JAK OCA].
*[[Protein phosphatase 3D structures|Protein phosphatase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Arrowsmith, C.]]
[[Category: Arrowsmith C]]
[[Category: Berg, S Van Den.]]
[[Category: Berglund H]]
[[Category: Berglund, H.]]
[[Category: Busam R]]
[[Category: Busam, R.]]
[[Category: Collins R]]
[[Category: Collins, R.]]
[[Category: Edwards A]]
[[Category: Edwards, A.]]
[[Category: Ericsson UB]]
[[Category: Ericsson, U B.]]
[[Category: Flodin S]]
[[Category: Flodin, S.]]
[[Category: Flores A]]
[[Category: Flores, A.]]
[[Category: Graslund S]]
[[Category: Graslund, S.]]
[[Category: Hallberg BM]]
[[Category: Hallberg, B M.]]
[[Category: Hammarstrom M]]
[[Category: Hammarstrom, M.]]
[[Category: Hogbom M]]
[[Category: Hogbom, M.]]
[[Category: Holmberg Schiavone L]]
[[Category: Johansson, I.]]
[[Category: Johansson I]]
[[Category: Karlberg, T.]]
[[Category: Karlberg T]]
[[Category: Kotenyova, T.]]
[[Category: Kotenyova T]]
[[Category: Lundgren, S.]]
[[Category: Lundgren S]]
[[Category: Magnusdottir, A.]]
[[Category: Magnusdottir A]]
[[Category: Moche, M.]]
[[Category: Moche M]]
[[Category: Nilsson, P.]]
[[Category: Nilsson P]]
[[Category: Nordlund, P.]]
[[Category: Nordlund P]]
[[Category: Nyman, T.]]
[[Category: Nyman T]]
[[Category: Ogg, D.]]
[[Category: Ogg D]]
[[Category: Persson, C.]]
[[Category: Persson C]]
[[Category: Sagemark, J.]]
[[Category: Sagemark J]]
[[Category: Schiavone, L Holmberg.]]
[[Category: Stenmark P]]
[[Category: Stenmark, P.]]
[[Category: Sundstrom M]]
[[Category: Sundstrom, M.]]
[[Category: Thorsell AG]]
[[Category: Thorsell, A G.]]
[[Category: Uppenberg J]]
[[Category: Uppenberg, J.]]
[[Category: Upsten M]]
[[Category: Upsten, M.]]
[[Category: Van Den Berg S]]
[[Category: Weigelt, J.]]
[[Category: Weigelt J]]
[[Category: Alternative splicing]]
[[Category: B56g]]
[[Category: Nuclear protein]]
[[Category: Phosphorylation]]
[[Category: Pp2a]]
[[Category: Pp2a regulatory subunit]]
[[Category: Ppp2r5c]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 08:36:35 2008''

Latest revision as of 12:36, 9 May 2024

Human PP2A regulatory subunit B56gHuman PP2A regulatory subunit B56g

Structural highlights

2jak is a 1 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 2.6Å
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]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The PP2A serine/threonine phosphatase regulates a plethora of cellular processes. In the cell the predominant form of the enzyme is a heterotrimer, formed by a core dimer composed of a catalytic and a scaffolding subunit, which assemble together with one of a range of different regulatory B subunits. Here, we present the first structure of a free non-complexed B subunit, B56 gamma. Comparison with the recent structures of a heterotrimeric complex and the core dimer reveals several significant conformational changes in the interface region between the B56 gamma and the core dimer. These allow for an assembly scheme of the PP2A holoenzyme to be put forth where B56 gamma first complexes with the scaffolding subunit and subsequently binds to the catalytic subunit and this induces the formation of a binding site for the invariant C-terminus of the catalytic subunit that locks in the complex as a last step of assembly.

The structure of the PP2A regulatory subunit B56 gamma: the remaining piece of the PP2A jigsaw puzzle.,Magnusdottir A, Stenmark P, Flodin S, Nyman T, Kotenyova T, Graslund S, Ogg D, Nordlund P Proteins. 2009 Jan;74(1):212-21. PMID:18618707[3]

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

See Also

References

  1. ↑ 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
  2. ↑ 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
  3. ↑ Magnusdottir A, Stenmark P, Flodin S, Nyman T, Kotenyova T, Graslund S, Ogg D, Nordlund P. The structure of the PP2A regulatory subunit B56 gamma: the remaining piece of the PP2A jigsaw puzzle. Proteins. 2009 Jan;74(1):212-21. PMID:18618707 doi:10.1002/prot.22150

2jak, resolution 2.60Å

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