2bcd: Difference between revisions

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-{{Seed}}
-[[Image:2bcd.png|left|200px]]
-<!--
+==X-ray crystal structure of Protein Phosphatase-1 with the marine toxin motuporin bound==
-The line below this paragraph, containing "STRUCTURE_2bcd", creates the "Structure Box" on the page.
+<StructureSection load='2bcd' size='340' side='right'caption='[[2bcd]], [[Resolution|resolution]] 2.10&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'>[[2bcd]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Theonella_sp. Theonella sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BCD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BCD 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]] 2.1&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=1ZN:(2S,3S,4E,6E,8S,9S)-3-AMINO-9-METHOXY-2,6,8-TRIMETHYL-10-PHENYLDECA-4,6-DIENOIC+ACID'>1ZN</scene>, <scene name='pdbligand=ACB:3-METHYL-BETA-D-ASPARTIC+ACID'>ACB</scene>, <scene name='pdbligand=BME:BETA-MERCAPTOETHANOL'>BME</scene>, <scene name='pdbligand=FGA:GAMMA-D-GLUTAMIC+ACID'>FGA</scene>, <scene name='pdbligand=MDH:N-METHYLDEHYDROBUTYRINE'>MDH</scene>, <scene name='pdbligand=MN:MANGANESE+(II)+ION'>MN</scene></td></tr>
-{{STRUCTURE_2bcd|  PDB=2bcd  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2bcd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bcd OCA], [https://pdbe.org/2bcd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bcd RCSB], [https://www.ebi.ac.uk/pdbsum/2bcd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bcd ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/PP1G_HUMAN PP1G_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. Dephosphorylates RPS6KB1. 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.<ref>PMID:17936702</ref> <ref>PMID:20516061</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/bc/2bcd_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=2bcd ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The microcystins and nodularins are tumour promoting hepatotoxins that are responsible for global adverse human health effects and wildlife fatalities in countries where drinking water supplies contain cyanobacteria. The toxins function by inhibiting broad specificity Ser/Thr protein phosphatases in the host cells, thereby disrupting signal transduction pathways. A previous crystal structure of a microcystin bound to the catalytic subunit of protein phosphatase-1 (PP-1c) showed distinct changes in the active site region when compared with protein phosphatase-1 structures bound to other toxins. We have elucidated the crystal structures of the cyanotoxins, motuporin (nodularin-V) and dihydromicrocystin-LA bound to human protein phosphatase-1c (gamma isoform). The atomic structures of these complexes reveal the structural basis for inhibition of protein phosphatases by these toxins. Comparisons of the structures of the cyanobacterial toxin:phosphatase complexes explain the biochemical mechanism by which microcystins but not nodularins permanently modify their protein phosphatase targets by covalent addition to an active site cysteine residue.
-===X-ray crystal structure of Protein Phosphatase-1 with the marine toxin motuporin bound===
+Crystal structures of protein phosphatase-1 bound to motuporin and dihydromicrocystin-LA: elucidation of the mechanism of enzyme inhibition by cyanobacterial toxins.,Maynes JT, Luu HA, Cherney MM, Andersen RJ, Williams D, Holmes CF, James MN J Mol Biol. 2006 Feb 10;356(1):111-20. Epub 2005 Nov 22. PMID:16343532<ref>PMID:16343532</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 2bcd" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_16343532}}, adds the Publication Abstract to the page
+*[[Elastase 3D structures|Elastase 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 16343532 is the PubMed ID number.
+== References ==
--->
+<references/>
-{{ABSTRACT_PUBMED_16343532}}
+__TOC__
+</StructureSection>
-==About this Structure==
-BCD is a 1 chain 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=2BCD OCA].
-==Reference==
-<ref group="xtra">PMID:16343532</ref><references group="xtra"/>
 [[Category: Homo sapiens]]
-[[Category: Phosphoprotein phosphatase]]
+[[Category: Large Structures]]
-[[Category: Andersen, R J.]]
+[[Category: Theonella sp]]
-[[Category: Cherney, M M.]]
+[[Category: Andersen RJ]]
-[[Category: Holmes, C F.]]
+[[Category: Cherney MM]]
-[[Category: James, M N.]]
+[[Category: Holmes CF]]
-[[Category: Luu, H A.]]
+[[Category: James MN]]
-[[Category: Maynes, J T.]]
+[[Category: Luu HA]]
-[[Category: Williams, D.]]
+[[Category: Maynes JT]]
-[[Category: Motuporin]]
+[[Category: Williams D]]
-[[Category: Natural product inhibitor]]
-[[Category: Nodularin]]
-[[Category: Protein phosphtase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 17:46:10 2009''