View source for 5xer


==TK9 NMR structure in DPC micelle==
<StructureSection load='5xer' size='340' side='right'caption='[[5xer]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5xer]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Severe_acute_respiratory_syndrome-related_coronavirus Severe acute respiratory syndrome-related coronavirus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5XER OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5XER FirstGlance]. <br>
</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=5xer FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5xer OCA], [https://pdbe.org/5xer PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5xer RCSB], [https://www.ebi.ac.uk/pdbsum/5xer PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5xer ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/VEMP_SARS VEMP_SARS] Plays a central role in virus morphogenesis and assembly. Acts as a viroporin and self-assembles in host membranes forming pentameric protein-lipid pores that allow ion transport. Also plays a role in the induction of apoptosis (By similarity). Activates the host NLRP3 inflammasome, leading to IL-1beta overproduction.[HAMAP-Rule:MF_04204]<ref>PMID:24788150</ref> <ref>PMID:26331680</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
In recent years, several studies based on the interaction of self-assembling short peptides derived from viroporins with model membranes, have improved our understanding of the molecular mechanism of corona virus (CoV) infection under physiological conditions. In this study, we have characterized the mechanism of membrane interaction of a short, 9-residue peptide TK9 (T(55)VYVYSRVK(63)) that had been derived from the carboxyl terminal of the Severe Acute Respiratory Syndrome (SARS) corona virus (SARS CoV) envelope (E) protein. The peptide has been studied for its physical changes in the presence of both zwitterionic DPC and negatively charged SDS model membrane micelles, respectively, with the help of a battery of biophysical techniques including two-dimensional solution state NMR spectroscopy. Interestingly, in both micellar environments, TK9 adopted an alpha helical conformation; however, the helical propensities were much higher in the case of DPC compared to those of SDS micelle, suggesting that TK9 has more specificity towards eukaryotic cell membrane than the bacterial cell membrane. The orientation of the peptide TK9 also varies in the different micellar environments. The peptide's affinity was further manifested by its pronounced membrane disruption ability towards the mammalian compared to the bacterial membrane mimic. Collectively, the in-depth structural information on the interaction of TK9 with different membrane environments explains the host specificity and membrane orientation owing to subsequent membrane disruption implicated in the viral pathogenesis.

Structural insights of a self-assembling 9-residue peptide from the C-terminal tail of the SARS corona virus E-protein in DPC and SDS micelles: A combined high and low resolution spectroscopic study.,Ghosh A, Bhattacharyya D, Bhunia A Biochim Biophys Acta Biomembr. 2018 Feb;1860(2):335-346. doi:, 10.1016/j.bbamem.2017.10.015. Epub 2017 Oct 14. PMID:29038024<ref>PMID:29038024</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5xer" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Severe acute respiratory syndrome-related coronavirus]]
[[Category: Bhunia A]]
[[Category: Ghosh A]]