3dyq

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{{Seed}}
 
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[[Image:3dyq.png|left|200px]]
 
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==human phosphodiestrase 9 (inhibited by omitting divalent cation) in complex with cGMP==
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The line below this paragraph, containing "STRUCTURE_3dyq", creates the "Structure Box" on the page.
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<StructureSection load='3dyq' size='340' side='right'caption='[[3dyq]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[3dyq]] 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=3DYQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3DYQ FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=IBM:3-ISOBUTYL-1-METHYLXANTHINE'>IBM</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene>, <scene name='pdbligand=PCG:CYCLIC+GUANOSINE+MONOPHOSPHATE'>PCG</scene></td></tr>
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{{STRUCTURE_3dyq| PDB=3dyq | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3dyq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3dyq OCA], [https://pdbe.org/3dyq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3dyq RCSB], [https://www.ebi.ac.uk/pdbsum/3dyq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3dyq ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PDE9A_HUMAN PDE9A_HUMAN] Hydrolyzes the second messenger cGMP, which is a key regulator of many important physiological processes.<ref>PMID:18757755</ref>
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dy/3dyq_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=3dyq ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The phosphodiesterases (PDEs) are metal ion-dependent enzymes that regulate cellular signaling by metabolic inactivation of the ubiquitous second messengers cAMP and cGMP. In this role, the PDEs are involved in many biological and metabolic processes and are proven targets of successful drugs for the treatments of a wide range of diseases. However, because of the rapidity of the hydrolysis reaction, an experimental knowledge of the enzymatic mechanisms of the PDEs at the atomic level is still lacking. Here, we report the structures of reaction intermediates accumulated at the reaction steady state in PDE9/crystal and preserved by freeze-trapping. These structures reveal the catalytic process of a PDE and explain the substrate specificity of PDE9 in an actual reaction and the cation requirements of PDEs in general.
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===human phosphodiestrase 9 (inhibited by omitting divalent cation) in complex with cGMP===
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Structural basis for the catalytic mechanism of human phosphodiesterase 9.,Liu S, Mansour MN, Dillman KS, Perez JR, Danley DE, Aeed PA, Simons SP, Lemotte PK, Menniti FS Proc Natl Acad Sci U S A. 2008 Sep 9;105(36):13309-14. Epub 2008 Aug 29. PMID:18757755<ref>PMID:18757755</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3dyq" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_18757755}}, adds the Publication Abstract to the page
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*[[Phosphodiesterase 3D structures|Phosphodiesterase 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 18757755 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_18757755}}
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__TOC__
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</StructureSection>
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==About this Structure==
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3DYQ is a 2 chains structure of sequences 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=3DYQ OCA].
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==Reference==
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<ref group="xtra">PMID:18757755</ref><references group="xtra"/>
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[[Category: 3',5'-cyclic-GMP phosphodiesterase]]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Danley, D.]]
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[[Category: Large Structures]]
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[[Category: Dillman, K.]]
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[[Category: Danley D]]
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[[Category: Liu, S.]]
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[[Category: Dillman K]]
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[[Category: Mansour,M N.]]
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[[Category: Liu S]]
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[[Category: Menniti, F.]]
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[[Category: Mansour MN]]
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[[Category: Perez, J.]]
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[[Category: Menniti F]]
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[[Category: Alternative splicing]]
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[[Category: Perez J]]
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[[Category: Cgmp]]
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[[Category: Crystallography]]
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[[Category: Enzyme mechanism]]
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[[Category: Hydrolase]]
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[[Category: Manganese]]
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[[Category: Metal-binding]]
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[[Category: Phosphodiesterase]]
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[[Category: Phosphoprotein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 18:22:50 2009''
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Current revision

human phosphodiestrase 9 (inhibited by omitting divalent cation) in complex with cGMP

PDB ID 3dyq

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