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10.1016/j.virusres.2020.198058 http://scihub22266oqcxt.onion/10.1016/j.virusres.2020.198058 C7282740!7282740 !32531235     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=32531235 &cmd=llinks): Failed to open stream: HTTP request failed! 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Role of the GTNGTKR motif in the N-terminal receptor-binding domain of the SARS-CoV-2 spike protein |pdf=|usr=}}{{32531235 }} gab.com Text Role of the GTNGTKR motif in the N-terminal receptor-binding domain of the SARS-CoV-2 spike protein JO: Virus Res http://www.kidney.de/pget.php?&tw=1&pmid=32531235 #FOAvip The 2019 novel coronavirus disease (COVID-19) that emerged in China has been declared as public health emergency of international concern by the World Health Organization and the causative pathogen was named severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). In this report, we analyzed the structural characteristics of the N-terminal domain of the S1 subunit (S1-NTD) of the SARS-CoV-2 spike protein in comparison to the SARS-CoV in particular, and to other viruses presenting similar characteristic in general. Given the severity and the wide and rapid spread of the SARS-CoV-2 infection, it is very likely that the virus recognizes other receptors/co-receptors besides the ACE2. The NTD of the SARS-CoV-2 contains a receptor-binding motif different from that of SARS-CoV, with some insertions that could confer to the new coronavirus new receptor binding abilities. In particular, motifs similar to the insertion 72GTNGTKR78 have been found in structural proteins of other viruses; and these motifs were located in putative regions involved in recognizing protein and sugar receptors, suggesting therefore that similar binding abilities could be displayed by the SARS-CoV-2 S1-NTD. Moreover, concerning the origin of these NTD insertions, our findings point towards an evolutionary acquisition rather than the hypothesis of an engineered virus. Twit Text FOAVip Role of the GTNGTKR motif in the N-terminal receptor-binding domain of the SARS-CoV-2 spike protein ????Virus Res http://www.kidney.de/pget.php?&tw=1&pmid=32531235 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32531235 #FOAvip English Wikipedia <ref>{{Cite pmid|32531235 }}</ref> Role of the GTNGTKR motif in the N-terminal receptor-binding domain of the SARS-CoV-2 spike protein #MMPMID32531235 Behloul N ; Baha S ; Shi R ; Meng J Virus Res 2020[Sep]; 286 (ä): 198058 PMID32531235 show ga The 2019 novel coronavirus disease (COVID-19) that emerged in China has been declared as public health emergency of international concern by the World Health Organization and the causative pathogen was named severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). In this report, we analyzed the structural characteristics of the N-terminal domain of the S1 subunit (S1-NTD) of the SARS-CoV-2 spike protein in comparison to the SARS-CoV in particular, and to other viruses presenting similar characteristic in general. Given the severity and the wide and rapid spread of the SARS-CoV-2 infection, it is very likely that the virus recognizes other receptors/co-receptors besides the ACE2. The NTD of the SARS-CoV-2 contains a receptor-binding motif different from that of SARS-CoV, with some insertions that could confer to the new coronavirus new receptor binding abilities. In particular, motifs similar to the insertion 72GTNGTKR78 have been found in structural proteins of other viruses; and these motifs were located in putative regions involved in recognizing protein and sugar receptors, suggesting therefore that similar binding abilities could be displayed by the SARS-CoV-2 S1-NTD. Moreover, concerning the origin of these NTD insertions, our findings point towards an evolutionary acquisition rather than the hypothesis of an engineered virus. |Amino Acid Sequence [MESH] |Angiotensin-Converting Enzyme 2 [MESH] |Animals [MESH] |Betacoronavirus/*chemistry/genetics/metabolism [MESH] |Binding Sites [MESH] |COVID-19 [MESH] |Chiroptera [MESH] |Coronavirus Infections/pathology/virology [MESH] |Evolution, Molecular [MESH] |Gene Expression [MESH] |Host-Pathogen Interactions/drug effects/genetics [MESH] |Humans [MESH] |Middle East Respiratory Syndrome Coronavirus/*chemistry/genetics/metabolism [MESH] |Models, Molecular [MESH] |Pandemics [MESH] |Peptidyl-Dipeptidase A/*chemistry/genetics/metabolism [MESH] |Pneumonia, Viral/pathology/virology [MESH] |Protein Binding [MESH] |Protein Conformation, alpha-Helical [MESH] |Protein Conformation, beta-Strand [MESH] |Protein Interaction Domains and Motifs [MESH] |Receptors, Virus/*chemistry/genetics/metabolism [MESH] |SARS-CoV-2 [MESH] |Sequence Alignment [MESH] |Severe acute respiratory syndrome-related coronavirus/*chemistry/genetics/metabolism [MESH] |Spike Glycoprotein, Coronavirus/*chemistry/genetics/metabolism [MESH] |Structural Homology, Protein [MESH] |Thermodynamics [MESH]Role of the GTNGTKR motif in the N-terminal receptor-binding domain of(epmc).pdf DeepDyve Pubget Overpricing