8wbb: Difference between revisions

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'''Unreleased structure'''


The entry 8wbb is ON HOLD  until Paper Publication
==CryoEM structure of non-structural protein 1 dimer from dengue virus type 4==
<StructureSection load='8wbb' size='340' side='right'caption='[[8wbb]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8wbb]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Dengue_virus_4_Philippines/H241/1956 Dengue virus 4 Philippines/H241/1956]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8WBB OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8WBB FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.9&#8491;</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=8wbb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8wbb OCA], [https://pdbe.org/8wbb PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8wbb RCSB], [https://www.ebi.ac.uk/pdbsum/8wbb PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8wbb ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Flaviviruses encode a conserved, membrane-associated nonstructural protein 1 (NS1) with replication and immune evasion functions. The current knowledge of secreted NS1 (sNS1) oligomers is based on several low-resolution structures, thus hindering the development of drugs and vaccines against flaviviruses. Here, we revealed that recombinant sNS1 from flaviviruses exists in a dynamic equilibrium of dimer-tetramer-hexamer states. Two DENV4 hexameric NS1 structures and several tetrameric NS1 structures from multiple flaviviruses were solved at atomic resolution by cryo-EM. The stacking of the tetrameric NS1 and hexameric NS1 is facilitated by the hydrophobic beta-roll and connector domains. Additionally, a triacylglycerol molecule located within the central cavity may play a role in stabilizing the hexamer. Based on differentiated interactions between the dimeric NS1, two distinct hexamer models (head-to-head and side-to-side hexamer) and the step-by-step assembly mechanisms of NS1 dimer into hexamer were proposed. We believe that our study sheds light on the understanding of the NS1 oligomerization and contributes to NS1-based therapies.


Authors:  
The step-by-step assembly mechanism of secreted flavivirus NS1 tetramer and hexamer captured at atomic resolution.,Pan Q, Jiao H, Zhang W, Chen Q, Zhang G, Yu J, Zhao W, Hu H Sci Adv. 2024 May 3;10(18):eadm8275. doi: 10.1126/sciadv.adm8275. Epub 2024 May , 1. PMID:38691607<ref>PMID:38691607</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 8wbb" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Dengue virus 4 Philippines/H241/1956]]
[[Category: Large Structures]]
[[Category: Hu HL]]
[[Category: Jiao HZ]]
[[Category: Pan Q]]
Retrieved from "https://proteopedia.org/8wbb"