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10.1073/pnas.2100425118 http://scihub22266oqcxt.onion/10.1073/pnas.2100425118 33903171!8126795!33903171     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       Proc+Natl+Acad+Sci+U+S+A 2021 ; 118 (19): ä Nephropedia Template TP {{tp|p=33903171|t=2021. Dual nature of human ACE2 glycosylation in binding to SARS-CoV-2 spike |pdf=|usr=}}{{33903171}} gab.com Text Dual nature of human ACE2 glycosylation in binding to SARS-CoV-2 spike JO: Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=33903171 #FOAvip Binding of the spike protein of SARS-CoV-2 to the human angiotensin-converting enzyme 2 (ACE2) receptor triggers translocation of the virus into cells. Both the ACE2 receptor and the spike protein are heavily glycosylated, including at sites near their binding interface. We built fully glycosylated models of the ACE2 receptor bound to the receptor binding domain (RBD) of the SARS-CoV-2 spike protein. Using atomistic molecular dynamics (MD) simulations, we found that the glycosylation of the human ACE2 receptor contributes substantially to the binding of the virus. Interestingly, the glycans at two glycosylation sites, N90 and N322, have opposite effects on spike protein binding. The glycan at the N90 site partly covers the binding interface of the spike RBD. Therefore, this glycan can interfere with the binding of the spike protein and protect against docking of the virus to the cell. By contrast, the glycan at the N322 site interacts tightly with the RBD of the ACE2-bound spike protein and strengthens the complex. Remarkably, the N322 glycan binds to a conserved region of the spike protein identified previously as a cryptic epitope for a neutralizing antibody. By mapping the glycan binding sites, our MD simulations aid in the targeted development of neutralizing antibodies and SARS-CoV-2 fusion inhibitors. Twit Text FOAVip Dual nature of human ACE2 glycosylation in binding to SARS-CoV-2 spike ????Proc Natl Acad Sci U S A http://www.kidney.de/pget.php?&tw=1&pmid=33903171 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=33903171 #FOAvip English Wikipedia <ref>{{Cite pmid|33903171}}</ref> Dual nature of human ACE2 glycosylation in binding to SARS-CoV-2 spike #MMPMID33903171 Mehdipour AR; Hummer G Proc Natl Acad Sci U S A 2021[May]; 118 (19): ä PMID33903171show ga Binding of the spike protein of SARS-CoV-2 to the human angiotensin-converting enzyme 2 (ACE2) receptor triggers translocation of the virus into cells. Both the ACE2 receptor and the spike protein are heavily glycosylated, including at sites near their binding interface. We built fully glycosylated models of the ACE2 receptor bound to the receptor binding domain (RBD) of the SARS-CoV-2 spike protein. Using atomistic molecular dynamics (MD) simulations, we found that the glycosylation of the human ACE2 receptor contributes substantially to the binding of the virus. Interestingly, the glycans at two glycosylation sites, N90 and N322, have opposite effects on spike protein binding. The glycan at the N90 site partly covers the binding interface of the spike RBD. Therefore, this glycan can interfere with the binding of the spike protein and protect against docking of the virus to the cell. By contrast, the glycan at the N322 site interacts tightly with the RBD of the ACE2-bound spike protein and strengthens the complex. Remarkably, the N322 glycan binds to a conserved region of the spike protein identified previously as a cryptic epitope for a neutralizing antibody. By mapping the glycan binding sites, our MD simulations aid in the targeted development of neutralizing antibodies and SARS-CoV-2 fusion inhibitors. |Angiotensin-Converting Enzyme 2/*metabolism[MESH] |Glycosylation[MESH] |Humans[MESH] |Molecular Dynamics Simulation[MESH] |Protein Binding[MESH] |SARS-CoV-2/metabolism[MESH] |Spike Glycoprotein, Coronavirus/*metabolism[MESH]Dual nature of human ACE2 glycosylation in binding to SARS-CoV-2 spike(epmc).pdf DeepDyve Pubget Overpricing