5ysx
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Structure of P domain of GII.2 Noroviruses== | |
| + | <StructureSection load='5ysx' size='340' side='right'caption='[[5ysx]], [[Resolution|resolution]] 1.20Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5ysx]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Norovirus_GII Norovirus GII]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5YSX OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5YSX 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]] 1.202Å</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=5ysx FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ysx OCA], [https://pdbe.org/5ysx PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ysx RCSB], [https://www.ebi.ac.uk/pdbsum/5ysx PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ysx ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/A0A2R3BZ02_9CALI A0A2R3BZ02_9CALI]  | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Background: During 2016-2017, the previously rare GII.P16-GII.2 norovirus suddenly emerged as the predominant genotype causing gastroenteritis outbreaks in China and other countries. Its origin, phylodynamics, and mechanism behind the predominance remain unclear. Methods: Bayesian phylogenetic analyses were performed on 180 full capsid and 150 polymerase sequences of 2016-2017 GII.P16-GII.2 noroviruses in China, and those for all publicly available GII.P16 and GII.2 sequences. Saliva-based histo-blood group antigen (HBGA) binding assays and crystal structural analysis were conducted by using the P proteins of 2016-2017 GII.P16-GII.2 noroviruses. Results: The reemerging GII.P16-GII.2 norovirus showed a rapid genetic diversification after its emergence in 2012-2013. The antigenicity and HBGA binding profile of the early 2016-2017 and pre-2016 GII.2 noroviruses were similar. A further variant with a single Val256Ile mutation and the conventionally orientated Asp382 in the VP1 protein showed an expanded HBGA-binding spectrum. Mutations on the surface of polymerase that could alter its function were seen, which may help to accelerate the VP1 gene evolution to 5.5 x 10-3 substitutions per site per year. This virus can be traced back to Pearl River Delta, China. Conclusions: Our findings provide new insights into GII.2 norovirus epidemics and highlight the necessity of enhanced global surveillance for potential epidemics of rare-genotype noroviruses. | ||
| - | + | Genetic Analysis of Reemerging GII.P16-GII.2 Noroviruses in 2016-2017 in China.,Ao Y, Cong X, Jin M, Sun X, Wei X, Wang J, Zhang Q, Song J, Yu J, Cui J, Qi J, Tan M, Duan Z J Infect Dis. 2018 Jun 5;218(1):133-143. doi: 10.1093/infdis/jiy182. PMID:29617875<ref>PMID:29617875</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category:  | + | </div> | 
| + | <div class="pdbe-citations 5ysx" style="background-color:#fffaf0;"></div> | ||
| + | |||
| + | ==See Also== | ||
| + | *[[Virus coat proteins 3D structures|Virus coat proteins 3D structures]] | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Norovirus GII]] | ||
| + | [[Category: Ao Y]] | ||
| + | [[Category: Duan Z]] | ||
Current revision
Structure of P domain of GII.2 Noroviruses
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