View source for 2jak


==Human PP2A regulatory subunit B56g==
<StructureSection load='2jak' size='340' side='right'caption='[[2jak]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
</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].
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== 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<ref>PMID:18618707</ref>

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

==See Also==
*[[Protein phosphatase 3D structures|Protein phosphatase 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Arrowsmith C]]
[[Category: Berglund H]]
[[Category: Busam R]]
[[Category: Collins R]]
[[Category: Edwards A]]
[[Category: Ericsson UB]]
[[Category: Flodin S]]
[[Category: Flores A]]
[[Category: Graslund S]]
[[Category: Hallberg BM]]
[[Category: Hammarstrom M]]
[[Category: Hogbom M]]
[[Category: Holmberg Schiavone L]]
[[Category: Johansson I]]
[[Category: Karlberg T]]
[[Category: Kotenyova T]]
[[Category: Lundgren S]]
[[Category: Magnusdottir A]]
[[Category: Moche M]]
[[Category: Nilsson P]]
[[Category: Nordlund P]]
[[Category: Nyman T]]
[[Category: Ogg D]]
[[Category: Persson C]]
[[Category: Sagemark J]]
[[Category: Stenmark P]]
[[Category: Sundstrom M]]
[[Category: Thorsell AG]]
[[Category: Uppenberg J]]
[[Category: Upsten M]]
[[Category: Van Den Berg S]]
[[Category: Weigelt J]]