5wz1
From Proteopedia
(Difference between revisions)
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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=5wz1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wz1 OCA], [http://pdbe.org/5wz1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wz1 RCSB], [http://www.ebi.ac.uk/pdbsum/5wz1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wz1 ProSAT]</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=5wz1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wz1 OCA], [http://pdbe.org/5wz1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wz1 RCSB], [http://www.ebi.ac.uk/pdbsum/5wz1 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wz1 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Zika virus (ZIKV) has emerged as major health concern, as ZIKV infection has been shown to be associated with microcephaly, severe neurological disease and possibly male sterility. As the largest protein component within the ZIKV replication complex, NS5 plays key roles in the life cycle and survival of the virus through its N-terminal methyltransferase (MTase) and C-terminal RNA-dependent RNA polymerase (RdRp) domains. Here, we present the crystal structures of ZIKV NS5 MTase in complex with an RNA cap analogue (m7GpppA) and the free NS5 RdRp. We have identified the conserved features of ZIKV NS5 MTase and RdRp structures that could lead to development of current antiviral inhibitors being used against flaviviruses, including dengue virus and West Nile virus, to treat ZIKV infection. These results should inform and accelerate the structure-based design of antiviral compounds against ZIKV. | ||
| + | |||
| + | The crystal structure of Zika virus NS5 reveals conserved drug targets.,Duan W, Song H, Wang H, Chai Y, Su C, Qi J, Shi Y, Gao GF EMBO J. 2017 Apr 3;36(7):919-933. doi: 10.15252/embj.201696241. Epub 2017 Mar 2. PMID:28254839<ref>PMID:28254839</ref> | ||
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| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 5wz1" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 04:16, 30 August 2017
Crystal structure of Zika virus NS5 methyltransferase bound to S-adenosyl-L-methionine
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Categories: Duan, W | Gao, G F | Qi, J | Shi, Y | Song, H | Methyltransferase | Mtase | Sam | Transferase | Zika virus
