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10.1038/s41598-021-83761-5 http://scihub22266oqcxt.onion/10.1038/s41598-021-83761-5 33619331!7900180!33619331     free     free     free Warning: file_get_contents(https://eutils.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&id=33619331&cmd=llinks): Failed to open stream: HTTP request failed! 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Serine 477 plays a crucial role in the interaction of the SARS-CoV-2 spike protein with the human receptor ACE2 |pdf=|usr=}}{{33619331}} gab.com Text Serine 477 plays a crucial role in the interaction of the SARS-CoV-2 spike protein with the human receptor ACE2 JO: Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=33619331 #FOAvip Since the worldwide outbreak of the infectious disease COVID-19, several studies have been published to understand the structural mechanism of the novel coronavirus SARS-CoV-2. During the infection process, the SARS-CoV-2 spike (S) protein plays a crucial role in the receptor recognition and cell membrane fusion process by interacting with the human angiotensin-converting enzyme 2 (hACE2) receptor. However, new variants of these spike proteins emerge as the virus passes through the disease reservoir. This poses a major challenge for designing a potent antigen for an effective immune response against the spike protein. Through a normal mode analysis (NMA) we identified the highly flexible region in the receptor binding domain (RBD) of SARS-CoV-2, starting from residue 475 up to residue 485. Structurally, the position S477 shows the highest flexibility among them. At the same time, S477 is hitherto the most frequently exchanged amino acid residue in the RBDs of SARS-CoV-2 mutants. Therefore, using MD simulations, we have investigated the role of S477 and its two frequent mutations (S477G and S477N) at the RBD during the binding to hACE2. We found that the amino acid exchanges S477G and S477N strengthen the binding of the SARS-COV-2 spike with the hACE2 receptor. Twit Text FOAVip Serine 477 plays a crucial role in the interaction of the SARS-CoV-2 spike protein with the human receptor ACE2 ????Sci Rep http://www.kidney.de/pget.php?&tw=1&pmid=33619331 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33619331 #FOAvip English Wikipedia <ref>{{Cite pmid|33619331}}</ref> Serine 477 plays a crucial role in the interaction of the SARS-CoV-2 spike protein with the human receptor ACE2 #MMPMID33619331 Singh A; Steinkellner G; Kochl K; Gruber K; Gruber CC Sci Rep 2021[Feb]; 11 (1): 4320 PMID33619331show ga Since the worldwide outbreak of the infectious disease COVID-19, several studies have been published to understand the structural mechanism of the novel coronavirus SARS-CoV-2. During the infection process, the SARS-CoV-2 spike (S) protein plays a crucial role in the receptor recognition and cell membrane fusion process by interacting with the human angiotensin-converting enzyme 2 (hACE2) receptor. However, new variants of these spike proteins emerge as the virus passes through the disease reservoir. This poses a major challenge for designing a potent antigen for an effective immune response against the spike protein. Through a normal mode analysis (NMA) we identified the highly flexible region in the receptor binding domain (RBD) of SARS-CoV-2, starting from residue 475 up to residue 485. Structurally, the position S477 shows the highest flexibility among them. At the same time, S477 is hitherto the most frequently exchanged amino acid residue in the RBDs of SARS-CoV-2 mutants. Therefore, using MD simulations, we have investigated the role of S477 and its two frequent mutations (S477G and S477N) at the RBD during the binding to hACE2. We found that the amino acid exchanges S477G and S477N strengthen the binding of the SARS-COV-2 spike with the hACE2 receptor. |*Molecular Dynamics Simulation[MESH] |Angiotensin-Converting Enzyme 2/chemistry/*metabolism[MESH] |Humans[MESH] |Spike Glycoprotein, Coronavirus/*chemistry/*metabolism[MESH]Serine 477 plays a crucial role in the interaction of the SARS-CoV-2 s(epmc).pdf DeepDyve Pubget Overpricing