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10.1038/s41594-020-00536-8 http://scihub22266oqcxt.onion/10.1038/s41594-020-00536-8 33177698!7718435!33177698     free     free     free Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 213.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 247.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Nat+Struct+Mol+Biol 2020 ; 27 (12): 1202-1208 Nephropedia Template TP {{tp|p=33177698|t=2020. Structure and drug binding of the SARS-CoV-2 envelope protein transmembrane domain in lipid bilayers |pdf=|usr=}}{{33177698}} gab.com Text Structure and drug binding of the SARS-CoV-2 envelope protein transmembrane domain in lipid bilayers JO: Nat Struct Mol Biol http://www.kidney.de/pget.php?&tw=1&pmid=33177698 #FOAvip 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. Twit Text FOAVip Structure and drug binding of the SARS-CoV-2 envelope protein transmembrane domain in lipid bilayers ????Nat Struct Mol Biol http://www.kidney.de/pget.php?&tw=1&pmid=33177698 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33177698 #FOAvip English Wikipedia <ref>{{Cite pmid|33177698}}</ref> Structure and drug binding of the SARS-CoV-2 envelope protein transmembrane domain in lipid bilayers #MMPMID33177698 Mandala VS; McKay MJ; Shcherbakov AA; Dregni AJ; Kolocouris A; Hong M Nat Struct Mol Biol 2020[Dec]; 27 (12): 1202-1208 PMID33177698show ga 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. |Amantadine/chemistry[MESH] |Amiloride/analogs & derivatives/chemistry[MESH] |Antiviral Agents/chemistry[MESH] |Coronavirus Envelope Proteins/*chemistry/genetics[MESH] |Dimyristoylphosphatidylcholine/chemistry[MESH] |Hydrogen-Ion Concentration[MESH] |Lipid Bilayers/*chemistry[MESH] |Magnetic Resonance Spectroscopy[MESH] |Models, Molecular[MESH] |Phenylalanine/chemistry[MESH] |Phospholipids/chemistry[MESH] |Protein Conformation[MESH] |Protein Domains[MESH]Structure and drug binding of the SARS-CoV-2 envelope protein transmem(epmc).pdf DeepDyve Pubget Overpricing