7bw6
From Proteopedia
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| - | ==== | + | ==Varicella-zoster virus capsid== |
| - | < | + | <SX load='7bw6' size='340' side='right' viewer='molstar' caption='[[7bw6]], [[Resolution|resolution]] 3.70Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id= OCA]. For a <b>guided tour on the structure components</b> use [ | + | <table><tr><td colspan='2'>[[7bw6]] is a 46 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_alphaherpesvirus_3 Human alphaherpesvirus 3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7BW6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7BW6 FirstGlance]. <br> |
| - | </td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.7Å</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=7bw6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7bw6 OCA], [https://pdbe.org/7bw6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7bw6 RCSB], [https://www.ebi.ac.uk/pdbsum/7bw6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7bw6 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/Q6QCL5_HHV3 Q6QCL5_HHV3] | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Varicella-zoster virus (VZV), a member of the Alphaherpesvirinae subfamily, causes severe diseases in humans of all ages. The viral capsids play critical roles in herpesvirus infection, making them potential antiviral targets. Here, we present the 3.7-A-resolution structure of the VZV A-capsid and define the molecular determinants underpinning the assembly of this complicated viral machinery. Overall, the VZV capsid has a similar architecture to that of other known herpesviruses. The major capsid protein (MCP) assembles into pentons and hexons, forming extensive intra- and inter-capsomer interaction networks that are further secured by the small capsid protein (SCP) and the heterotriplex. The structure reveals a pocket beneath the floor of MCP that could potentially be targeted by antiviral inhibitors. In addition, we identified two alphaherpesvirus-specific structural features in SCP and Tri1 proteins. These observations highlight the divergence of different herpesviruses and provide an important basis for developing antiviral drugs. | ||
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| + | Cryo-EM structure of the varicella-zoster virus A-capsid.,Sun J, Liu C, Peng R, Zhang FK, Tong Z, Liu S, Shi Y, Zhao Z, Zeng WB, Gao GF, Shen HJ, Yang X, Luo M, Qi J, Wang P Nat Commun. 2020 Sep 22;11(1):4795. doi: 10.1038/s41467-020-18537-y. PMID:32963252<ref>PMID:32963252</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 7bw6" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
| - | </ | + | </SX> |
| + | [[Category: Human alphaherpesvirus 3]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
| - | [[Category: | + | [[Category: Liu CC]] |
| + | [[Category: Qi JX]] | ||
| + | [[Category: Sun JQ]] | ||
| + | [[Category: Wang PY]] | ||
Current revision
Varicella-zoster virus capsid
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