7k3g: Difference between revisions
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New page: '''Unreleased structure''' The entry 7k3g is ON HOLD Authors: Mandala, V.S., Hong, M., McKay, M.J., Shcherbakov, A.S., Dregni, A.J. Description: SARS-CoV-2 Envelope Protein Transmembra... |
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==SARS-CoV-2 Envelope Protein Transmembrane Domain: Pentameric Structure Determined by Solid-State NMR== | |||
<StructureSection load='7k3g' size='340' side='right'caption='[[7k3g]]' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7k3g]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Severe_acute_respiratory_syndrome_coronavirus_2 Severe acute respiratory syndrome coronavirus 2]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7K3G OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7K3G 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=7k3g FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7k3g OCA], [https://pdbe.org/7k3g PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7k3g RCSB], [https://www.ebi.ac.uk/pdbsum/7k3g PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7k3g ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/VEMP_SARS2 VEMP_SARS2] 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.[HAMAP-Rule:MF_04204] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
An essential protein of the SARS-CoV-2 virus, the envelope protein E, forms a homopentameric cation channel that is important for virus pathogenicity. Here we report a 2.1-A structure and the drug-binding site of E's transmembrane domain (ETM), determined using solid-state NMR spectroscopy. In lipid bilayers that mimic the endoplasmic reticulum-Golgi intermediate compartment (ERGIC) membrane, ETM forms a five-helix bundle surrounding a narrow pore. The protein deviates from the ideal alpha-helical geometry due to three phenylalanine residues, which stack within each helix and between helices. Together with valine and leucine interdigitation, these cause a dehydrated pore compared with the viroporins of influenza viruses and HIV. Hexamethylene amiloride binds the polar amino-terminal lumen, whereas acidic pH affects the carboxy-terminal conformation. Thus, the N- and C-terminal halves of this bipartite channel may interact with other viral and host proteins semi-independently. The structure sets the stage for designing E inhibitors as antiviral drugs. | |||
Structure and drug binding of the SARS-CoV-2 envelope protein transmembrane domain in lipid bilayers.,Mandala VS, McKay MJ, Shcherbakov AA, Dregni AJ, Kolocouris A, Hong M Nat Struct Mol Biol. 2020 Nov 11. pii: 10.1038/s41594-020-00536-8. doi:, 10.1038/s41594-020-00536-8. PMID:33177698<ref>PMID:33177698</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 7k3g" style="background-color:#fffaf0;"></div> | ||
[[Category: | == References == | ||
[[Category: Mandala | <references/> | ||
[[Category: | __TOC__ | ||
[[Category: | </StructureSection> | ||
[[Category: Large Structures]] | |||
[[Category: Severe acute respiratory syndrome coronavirus 2]] | |||
[[Category: Dregni AJ]] | |||
[[Category: Hong M]] | |||
[[Category: Mandala VS]] | |||
[[Category: McKay MJ]] | |||
[[Category: Shcherbakov AS]] | |||
