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10.1038/s41467-022-28654-5 http://scihub22266oqcxt.onion/10.1038/s41467-022-28654-5 35194049!8863989!35194049     free     free     free Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 211.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Nat+Commun 2022 ; 13 (1): 1002 Nephropedia Template TP {{tp|p=35194049|t=2022. Cooperative multivalent receptor binding promotes exposure of the SARS-CoV-2 fusion machinery core |pdf=|usr=}}{{35194049}} gab.com Text Cooperative multivalent receptor binding promotes exposure of the SARS-CoV-2 fusion machinery core JO: Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=35194049 #FOAvip The molecular events that permit the spike glycoprotein of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) to bind and enter cells are important to understand for both fundamental and therapeutic reasons. Spike proteins consist of S1 and S2 domains, which recognize angiotensin-converting enzyme 2 (ACE2) receptors and contain the viral fusion machinery, respectively. Ostensibly, the binding of spike trimers to ACE2 receptors promotes dissociation of the S1 domains and exposure of the fusion machinery, although the molecular details of this process have yet to be observed. We report the development of bottom-up coarse-grained (CG) models consistent with cryo-electron tomography data, and the use of CG molecular dynamics simulations to investigate viral binding and S2 core exposure. We show that spike trimers cooperatively bind to multiple ACE2 dimers at virion-cell interfaces in a manner distinct from binding between soluble proteins, which processively induces S1 dissociation. We also simulate possible variant behavior using perturbed CG models, and find that ACE2-induced S1 dissociation is primarily sensitive to conformational state populations and the extent of S1/S2 cleavage, rather than ACE2 binding affinity. These simulations reveal an important concerted interaction between spike trimers and ACE2 dimers that primes the virus for membrane fusion and entry. Twit Text FOAVip Cooperative multivalent receptor binding promotes exposure of the SARS-CoV-2 fusion machinery core ????Nat Commun http://www.kidney.de/pget.php?&tw=1&pmid=35194049 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=35194049 #FOAvip English Wikipedia <ref>{{Cite pmid|35194049}}</ref> Cooperative multivalent receptor binding promotes exposure of the SARS-CoV-2 fusion machinery core #MMPMID35194049 Pak AJ; Yu A; Ke Z; Briggs JAG; Voth GA Nat Commun 2022[Feb]; 13 (1): 1002 PMID35194049show ga The molecular events that permit the spike glycoprotein of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) to bind and enter cells are important to understand for both fundamental and therapeutic reasons. Spike proteins consist of S1 and S2 domains, which recognize angiotensin-converting enzyme 2 (ACE2) receptors and contain the viral fusion machinery, respectively. Ostensibly, the binding of spike trimers to ACE2 receptors promotes dissociation of the S1 domains and exposure of the fusion machinery, although the molecular details of this process have yet to be observed. We report the development of bottom-up coarse-grained (CG) models consistent with cryo-electron tomography data, and the use of CG molecular dynamics simulations to investigate viral binding and S2 core exposure. We show that spike trimers cooperatively bind to multiple ACE2 dimers at virion-cell interfaces in a manner distinct from binding between soluble proteins, which processively induces S1 dissociation. We also simulate possible variant behavior using perturbed CG models, and find that ACE2-induced S1 dissociation is primarily sensitive to conformational state populations and the extent of S1/S2 cleavage, rather than ACE2 binding affinity. These simulations reveal an important concerted interaction between spike trimers and ACE2 dimers that primes the virus for membrane fusion and entry. |Algorithms[MESH] |Angiotensin-Converting Enzyme 2/chemistry/*metabolism[MESH] |COVID-19/*metabolism/virology[MESH] |Host-Pathogen Interactions[MESH] |Humans[MESH] |Membrane Fusion[MESH] |Molecular Dynamics Simulation[MESH] |Protein Binding[MESH] |Protein Domains[MESH] |Protein Multimerization[MESH] |Receptors, Virus/chemistry/*metabolism[MESH] |SARS-CoV-2/*metabolism/physiology[MESH] |Spike Glycoprotein, Coronavirus/chemistry/*metabolism[MESH] |Virus Attachment[MESH]Cooperative multivalent receptor binding promotes exposure of the SARS(epmc).pdf DeepDyve Pubget Overpricing