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10.1016/j.bpc.2020.106420 http://scihub22266oqcxt.onion/10.1016/j.bpc.2020.106420 C7322478!7322478 !32622243     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=32622243 &cmd=llinks): Failed to open stream: HTTP request failed! 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Delving deep into the structural aspects of a furin cleavage site inserted into the spike protein of SARS-CoV-2: A structural biophysical perspective |pdf=|usr=}}{{32622243 }} gab.com Text Delving deep into the structural aspects of a furin cleavage site inserted into the spike protein of SARS-CoV-2: A structural biophysical perspective JO: Biophys Chem http://www.kidney.de/pget.php?&tw=1&pmid=32622243 #FOAvip One notable feature of the SARS-CoV-2 genome, the spike (S) protein of SARS-CoV-2 has a polybasic furin cleavage site (FCS) at its S1-S2 boundary through the insertion of 12 nucleotides encoding four amino acid residues PRRA. Quite intriguingly, this polybasic FCS is absent in coronaviruses of the same clade as SARS-CoV-2. Thus, with currently available experimental structural data for S protein, this short article presents a set of comprehensive structural characterization of the insertion of FCS into S protein, and argues against a hypothesis of the origin of SARS-CoV-2 from purposeful manipulation: (1), the inserted FCS is spatially located at a random coil loop region, mostly distantly solvent-exposed (instead of deeply buried), with no structural proximity to the other part of the S protein; (2), the insertion of FCS itself does not alter, neither stabilize nor de-stabilize, the three-dimensional structure of S; (3), the net result here is the insertion of a furin cleavage site into S protein, whose S1 and S2 subunits will still be strongly electrostatically bonded together from a structural and biophysical point of view, even if the polybasic FCS is actually cleaved by furin protease before or after viral cell entry. Twit Text FOAVip Delving deep into the structural aspects of a furin cleavage site inserted into the spike protein of SARS-CoV-2: A structural biophysical perspective ????Biophys Chem http://www.kidney.de/pget.php?&tw=1&pmid=32622243 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32622243 #FOAvip English Wikipedia <ref>{{Cite pmid|32622243 }}</ref> Delving deep into the structural aspects of a furin cleavage site inserted into the spike protein of SARS-CoV-2: A structural biophysical perspective #MMPMID32622243 Li W Biophys Chem 2020[Sep]; 264 (ä): 106420 PMID32622243 show ga One notable feature of the SARS-CoV-2 genome, the spike (S) protein of SARS-CoV-2 has a polybasic furin cleavage site (FCS) at its S1-S2 boundary through the insertion of 12 nucleotides encoding four amino acid residues PRRA. Quite intriguingly, this polybasic FCS is absent in coronaviruses of the same clade as SARS-CoV-2. Thus, with currently available experimental structural data for S protein, this short article presents a set of comprehensive structural characterization of the insertion of FCS into S protein, and argues against a hypothesis of the origin of SARS-CoV-2 from purposeful manipulation: (1), the inserted FCS is spatially located at a random coil loop region, mostly distantly solvent-exposed (instead of deeply buried), with no structural proximity to the other part of the S protein; (2), the insertion of FCS itself does not alter, neither stabilize nor de-stabilize, the three-dimensional structure of S; (3), the net result here is the insertion of a furin cleavage site into S protein, whose S1 and S2 subunits will still be strongly electrostatically bonded together from a structural and biophysical point of view, even if the polybasic FCS is actually cleaved by furin protease before or after viral cell entry. |Amino Acid Sequence [MESH] |Betacoronavirus/*chemistry/genetics [MESH] |Furin/*chemistry [MESH] |Gene Expression [MESH] |Humans [MESH] |Hydrogen Bonding [MESH] |Models, Molecular [MESH] |Protein Conformation, alpha-Helical [MESH] |Protein Conformation, beta-Strand [MESH] |Protein Interaction Domains and Motifs [MESH] |Proteolysis [MESH] |SARS-CoV-2 [MESH] |Spike Glycoprotein, Coronavirus/*chemistry/genetics/metabolism [MESH]Delving deep into the structural aspects of a furin cleavage site inse(epmc).pdf DeepDyve Pubget Overpricing