5dus

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==Crystal structure of MERS-CoV macro domain in complex with ADP-ribose==
==Crystal structure of MERS-CoV macro domain in complex with ADP-ribose==
<StructureSection load='5dus' size='340' side='right' caption='[[5dus]], [[Resolution|resolution]] 1.43&Aring;' scene=''>
<StructureSection load='5dus' size='340' side='right' caption='[[5dus]], [[Resolution|resolution]] 1.43&Aring;' scene=''>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5dus FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dus OCA], [http://pdbe.org/5dus PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dus RCSB], [http://www.ebi.ac.uk/pdbsum/5dus PDBsum]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5dus FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5dus OCA], [http://pdbe.org/5dus PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5dus RCSB], [http://www.ebi.ac.uk/pdbsum/5dus PDBsum]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The newly emerging Middle East respiratory syndrome coronavirus (MERS-CoV) encodes the conserved macro domain within non-structural protein 3. However, the precise biochemical function and structure of the macro domain is unclear. Using differential scanning fluorimetry and isothermal titration calorimetry, we characterized the MERS-CoV macro domain as a more efficient adenosine diphosphate (ADP)-ribose binding module than macro domains from other CoVs. Furthermore, the crystal structure of the MERS-CoV macro domain was determined at 1.43-A resolution in complex with ADP-ribose. Comparison of macro domains from MERS-CoV and other human CoVs revealed structural differences in the alpha1 helix alters how the conserved Asp-20 interacts with ADP-ribose and may explain the efficient binding of the MERS-CoV macro domain to ADP-ribose. This study provides structural and biophysical bases to further evaluate the role of the MERS-CoV macro domain in the host response via ADP-ribose binding but also as a potential target for drug design.
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Macro Domain from Middle East Respiratory Syndrome Coronavirus (MERS-CoV) Is an Efficient ADP-ribose Binding Module: CRYSTAL STRUCTURE AND BIOCHEMICAL STUDIES.,Cho CC, Lin MH, Chuang CY, Hsu CH J Biol Chem. 2016 Mar 4;291(10):4894-902. doi: 10.1074/jbc.M115.700542. Epub 2016, Jan 5. PMID:26740631<ref>PMID:26740631</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 5dus" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Revision as of 18:51, 10 May 2016

Crystal structure of MERS-CoV macro domain in complex with ADP-ribose

5dus, resolution 1.43Å

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