1s1d

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[[Image:1s1d.png|left|200px]]
 
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{{STRUCTURE_1s1d| PDB=1s1d | SCENE= }}
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==Structure and protein design of human apyrase==
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<StructureSection load='1s1d' size='340' side='right'caption='[[1s1d]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1s1d]] 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=1S1D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1S1D FirstGlance]. <br>
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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]] 1.6&#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=GP2:PHOSPHOMETHYLPHOSPHONIC+ACID+GUANOSYL+ESTER'>GP2</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=TRS:2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>TRS</scene></td></tr>
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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=1s1d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1s1d OCA], [https://pdbe.org/1s1d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1s1d RCSB], [https://www.ebi.ac.uk/pdbsum/1s1d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1s1d ProSAT]</span></td></tr>
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</table>
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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/s1/1s1d_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=1s1d 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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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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===Structure and protein design of human apyrase===
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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:15006348<ref>PMID:15006348</ref>
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{{ABSTRACT_PUBMED_15006348}}
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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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==About this Structure==
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<div class="pdbe-citations 1s1d" style="background-color:#fffaf0;"></div>
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[[1s1d]] is a 2 chain structure with 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=1S1D OCA].
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== References ==
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<references/>
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==Reference==
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__TOC__
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<ref group="xtra">PMID:015006348</ref><references group="xtra"/>
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</StructureSection>
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[[Category: Apyrase]]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Dai, J.]]
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[[Category: Large Structures]]
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[[Category: Deng, Y.]]
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[[Category: Dai J]]
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[[Category: Liu, J.]]
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[[Category: Deng Y]]
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[[Category: Lu, M.]]
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[[Category: Liu J]]
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[[Category: Smith, T M.]]
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[[Category: Lu M]]
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[[Category: Adpase]]
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[[Category: Smith TM]]
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[[Category: Calcium-binding protein]]
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[[Category: Five-blade beta propeller]]
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[[Category: Hydrolase]]
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[[Category: Nucleotide-binding motif]]
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Current revision

Structure and protein design of human apyrase

PDB ID 1s1d

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