1s18

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(New page: 200px<br /> <applet load="1s18" size="450" color="white" frame="true" align="right" spinBox="true" caption="1s18, resolution 1.70&Aring;" /> '''Structure and prote...)
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[[Image:1s18.gif|left|200px]]<br />
 
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<applet load="1s18" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1s18, resolution 1.70&Aring;" />
 
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'''Structure and protein design of human apyrase'''<br />
 
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==Overview==
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==Structure and protein design of human apyrase==
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Hematophagous arthropods secrete a salivary apyrase that inhibits platelet, activation by catabolizing ADP released from damaged tissues and blood, cells. We report the X-ray crystal structures of a human enzyme of the, soluble apyrase family in its apo state and bound to a substrate analog., The structures reveal a nucleotide binding domain comprising a five-blade, beta propeller, binding determinants of the substrate and the active site, and an unusual calcium binding site with a potential regulatory function., Using a comparative structural biology approach, we were able to redesign, the human apyrase so as to enhance its ADPase activity by more than, 100-fold. The engineered enzyme is a potent inhibitor of platelet, aggregation and may serve as the basis for the development of a new class, of antithrombotic agents.
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<StructureSection load='1s18' size='340' side='right'caption='[[1s18]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1s18]] 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=1S18 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S18 FirstGlance]. <br>
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1S18 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 CA, ACT and TRS as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Apyrase Apyrase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.1.5 3.6.1.5] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1S18 OCA].
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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]] 1.7&#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=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
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==Reference==
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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=1s18 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s18 OCA], [https://pdbe.org/1s18 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s18 RCSB], [https://www.ebi.ac.uk/pdbsum/1s18 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s18 ProSAT]</span></td></tr>
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Structure and protein design of a human platelet function inhibitor., Dai J, Liu J, Deng Y, Smith TM, Lu M, Cell. 2004 Mar 5;116(5):649-59. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15006348 15006348]
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</table>
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[[Category: Apyrase]]
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== Disease ==
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[https://www.uniprot.org/uniprot/CANT1_HUMAN CANT1_HUMAN] Desbuquois syndrome. The disease is caused by mutations affecting the gene represented in this entry.
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== Function ==
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[https://www.uniprot.org/uniprot/CANT1_HUMAN CANT1_HUMAN] Calcium-dependent nucleotidase with a preference for UDP. The order of activity with different substrates is UDP > GDP > UTP > GTP. Has very low activity towards ADP and even lower activity towards ATP. Does not hydrolyze AMP and GMP. Involved in proteoglycan synthesis.<ref>PMID:12234496</ref> <ref>PMID:15248776</ref> <ref>PMID:22539336</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/s1/1s18_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=1s18 ConSurf].
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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[[Category: Dai, J.]]
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[[Category: Dai J]]
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[[Category: Deng, Y.]]
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[[Category: Deng Y]]
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[[Category: Liu, J.]]
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[[Category: Liu J]]
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[[Category: Lu, M.]]
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[[Category: Lu M]]
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[[Category: Smith, T.M.]]
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[[Category: Smith TM]]
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[[Category: ACT]]
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[[Category: CA]]
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[[Category: TRS]]
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[[Category: adpase]]
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[[Category: calcium-binding protein]]
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[[Category: five-blade beta propeller]]
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[[Category: nucleotide-binding motif]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:09:07 2007''
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Current revision

Structure and protein design of human apyrase

PDB ID 1s18

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