2ouu: Difference between revisions

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New page: left|200px<br /> <applet load="2ouu" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ouu, resolution 1.52Å" /> '''crystal structure o...
 
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[[Image:2ouu.gif|left|200px]]<br />
<applet load="2ouu" size="450" color="white" frame="true" align="right" spinBox="true"
caption="2ouu, resolution 1.52&Aring;" />
'''crystal structure of PDE10A2 mutant D674A in complex with cGMP'''<br />


==Overview==
==crystal structure of PDE10A2 mutant D674A in complex with cGMP==
Phosphodiesterases (PDEs) hydrolyze the second messengers cAMP and cGMP., It remains unknown how individual PDE families selectively recognize cAMP, and cGMP. This work reports structural studies on substrate specificity., The crystal structures of the catalytic domains of the D674A and D564N, mutants of PDE10A2 in complex with cAMP and cGMP reveal that two, substrates bind to the active site with the same syn configuration but, different orientations and interactions. The products AMP and GMP bind, PDE10A2 with the anti configuration and interact with both divalent, metals, in contrast to no direct contact of the substrates. The structures, suggest that the syn configurations of cAMP and cGMP are the genuine, substrates for PDE10 and the specificity is achieved through the different, interactions and conformations of the substrates. The PDE10A2 structures, also show that the conformation of the invariant glutamine is locked by, two hydrogen bonds and is unlikely to switch for substrate recognition., Sequence alignment shows a potential pocket, in which variation of amino, acids across PDE families defines the size and shape of the pocket and, thus determines the substrate specificity.
<StructureSection load='2ouu' size='340' side='right'caption='[[2ouu]], [[Resolution|resolution]] 1.52&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2ouu]] 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=2OUU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2OUU 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]] 1.52&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=35G:GUANOSINE-3,5-MONOPHOSPHATE'>35G</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene></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=2ouu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ouu OCA], [https://pdbe.org/2ouu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ouu RCSB], [https://www.ebi.ac.uk/pdbsum/2ouu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ouu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/PDE10_HUMAN PDE10_HUMAN] Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. Can hydrolyze both cAMP and cGMP, but has higher affinity for cAMP and is more efficient with cAMP as substrate.<ref>PMID:17389385</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/ou/2ouu_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=2ouu ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
2OUU is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MG and 35G as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/3',5'-cyclic-nucleotide_phosphodiesterase 3',5'-cyclic-nucleotide phosphodiesterase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.4.17 3.1.4.17] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2OUU OCA].
*[[Phosphodiesterase 3D structures|Phosphodiesterase 3D structures]]
 
== References ==
==Reference==
<references/>
Structural insight into substrate specificity of phosphodiesterase 10., Wang H, Liu Y, Hou J, Zheng M, Robinson H, Ke H, Proc Natl Acad Sci U S A. 2007 Apr 3;104(14):5782-7. Epub 2007 Mar 26. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17389385 17389385]
__TOC__
[[Category: 3',5'-cyclic-nucleotide phosphodiesterase]]
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Hou, J.]]
[[Category: Hou J]]
[[Category: Liu, Y.D.]]
[[Category: Liu YD]]
[[Category: Robinson, H.]]
[[Category: Robinson H]]
[[Category: Wang, H.C.]]
[[Category: Wang HC]]
[[Category: Zheng, M.Y.]]
[[Category: Zheng MY]]
[[Category: 35G]]
[[Category: MG]]
[[Category: cgmp]]
[[Category: pde]]
[[Category: substrate specificity]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 23:16:34 2007''

Latest revision as of 12:06, 21 February 2024

crystal structure of PDE10A2 mutant D674A in complex with cGMPcrystal structure of PDE10A2 mutant D674A in complex with cGMP

Structural highlights

2ouu 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 1.52Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

PDE10_HUMAN Plays a role in signal transduction by regulating the intracellular concentration of cyclic nucleotides. Can hydrolyze both cAMP and cGMP, but has higher affinity for cAMP and is more efficient with cAMP as substrate.[1]

Evolutionary Conservation

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

See Also

References

  1. ↑ Wang H, Liu Y, Hou J, Zheng M, Robinson H, Ke H. Structural insight into substrate specificity of phosphodiesterase 10. Proc Natl Acad Sci U S A. 2007 Apr 3;104(14):5782-7. Epub 2007 Mar 26. PMID:17389385

2ouu, resolution 1.52Å

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