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10.1038/s41557-021-00758-3 http://scihub22266oqcxt.onion/10.1038/s41557-021-00758-3 34413500!8488004!34413500     free     free     free Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\34413500.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Nat+Chem 2021 ; 13 (10): 963-968 Nephropedia Template TP {{tp|p=34413500|t=2021. A glycan gate controls opening of the SARS-CoV-2 spike protein |pdf=|usr=}}{{34413500}} gab.com Text A glycan gate controls opening of the SARS-CoV-2 spike protein JO: Nat Chem http://www.kidney.de/pget.php?&tw=1&pmid=34413500 #FOAvip SARS-CoV-2 infection is controlled by the opening of the spike protein receptor binding domain (RBD), which transitions from a glycan-shielded 'down' to an exposed 'up' state to bind the human angiotensin-converting enzyme 2 receptor and infect cells. While snapshots of the 'up' and 'down' states have been obtained by cryo-electron microscopy and cryo-electron tomagraphy, details of the RBD-opening transition evade experimental characterization. Here over 130 micros of weighted ensemble simulations of the fully glycosylated spike ectodomain allow us to characterize more than 300 continuous, kinetically unbiased RBD-opening pathways. Together with ManifoldEM analysis of cryo-electron microscopy data and biolayer interferometry experiments, we reveal a gating role for the N-glycan at position N343, which facilitates RBD opening. Residues D405, R408 and D427 also participate. The atomic-level characterization of the glycosylated spike activation mechanism provided herein represents a landmark study for ensemble pathway simulations and offers a foundation for understanding the fundamental mechanisms of SARS-CoV-2 viral entry and infection. Twit Text FOAVip A glycan gate controls opening of the SARS-CoV-2 spike protein ????Nat Chem http://www.kidney.de/pget.php?&tw=1&pmid=34413500 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=34413500 #FOAvip English Wikipedia <ref>{{Cite pmid|34413500}}</ref> A glycan gate controls opening of the SARS-CoV-2 spike protein #MMPMID34413500 Sztain T; Ahn SH; Bogetti AT; Casalino L; Goldsmith JA; Seitz E; McCool RS; Kearns FL; Acosta-Reyes F; Maji S; Mashayekhi G; McCammon JA; Ourmazd A; Frank J; McLellan JS; Chong LT; Amaro RE Nat Chem 2021[Oct]; 13 (10): 963-968 PMID34413500show ga SARS-CoV-2 infection is controlled by the opening of the spike protein receptor binding domain (RBD), which transitions from a glycan-shielded 'down' to an exposed 'up' state to bind the human angiotensin-converting enzyme 2 receptor and infect cells. While snapshots of the 'up' and 'down' states have been obtained by cryo-electron microscopy and cryo-electron tomagraphy, details of the RBD-opening transition evade experimental characterization. Here over 130 micros of weighted ensemble simulations of the fully glycosylated spike ectodomain allow us to characterize more than 300 continuous, kinetically unbiased RBD-opening pathways. Together with ManifoldEM analysis of cryo-electron microscopy data and biolayer interferometry experiments, we reveal a gating role for the N-glycan at position N343, which facilitates RBD opening. Residues D405, R408 and D427 also participate. The atomic-level characterization of the glycosylated spike activation mechanism provided herein represents a landmark study for ensemble pathway simulations and offers a foundation for understanding the fundamental mechanisms of SARS-CoV-2 viral entry and infection. |Cryoelectron Microscopy[MESH] |Humans[MESH] |Molecular Dynamics Simulation[MESH] |Polysaccharides/*metabolism[MESH]A glycan gate controls opening of the SARS-CoV-2 spike protein (epmc).pdf DeepDyve Pubget Overpricing