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10.7554/eLife.75720 http://scihub22266oqcxt.onion/10.7554/eLife.75720 35323112!8963885!35323112     free     free     free Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 219.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Elife 2022 ; 11 (ä): ä Nephropedia Template TP {{tp|p=35323112|t=2022. The inherent flexibility of receptor binding domains in SARS-CoV-2 spike protein |pdf=|usr=}}{{35323112}} gab.com Text The inherent flexibility of receptor binding domains in SARS-CoV-2 spike protein JO: Elife http://www.kidney.de/pget.php?&tw=1&pmid=35323112 #FOAvip Spike (S) protein is the primary antigenic target for neutralization and vaccine development for the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). It decorates the virus surface and undergoes large motions of its receptor binding domains (RBDs) to enter the host cell. Here, we observe Down, one-Up, one-Open, and two-Up-like structures in enhanced molecular dynamics simulations, and characterize the transition pathways via inter-domain interactions. Transient salt-bridges between RBD(A) and RBD(C) and the interaction with glycan at N343(B) support RBD(A) motions from Down to one-Up. Reduced interactions between RBD(A) and RBD(B) in one-Up induce RBD(B) motions toward two-Up. The simulations overall agree with cryo-electron microscopy structure distributions and FRET experiments and provide hidden functional structures, namely, intermediates along Down-to-one-Up transition with druggable cryptic pockets as well as one-Open with a maximum exposed RBD. The inherent flexibility of S-protein thus provides essential information for antiviral drug rational design or vaccine development. Twit Text FOAVip The inherent flexibility of receptor binding domains in SARS-CoV-2 spike protein ????Elife http://www.kidney.de/pget.php?&tw=1&pmid=35323112 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=35323112 #FOAvip English Wikipedia <ref>{{Cite pmid|35323112}}</ref> The inherent flexibility of receptor binding domains in SARS-CoV-2 spike protein #MMPMID35323112 Dokainish HM; Re S; Mori T; Kobayashi C; Jung J; Sugita Y Elife 2022[Mar]; 11 (ä): ä PMID35323112show ga Spike (S) protein is the primary antigenic target for neutralization and vaccine development for the severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2). It decorates the virus surface and undergoes large motions of its receptor binding domains (RBDs) to enter the host cell. Here, we observe Down, one-Up, one-Open, and two-Up-like structures in enhanced molecular dynamics simulations, and characterize the transition pathways via inter-domain interactions. Transient salt-bridges between RBD(A) and RBD(C) and the interaction with glycan at N343(B) support RBD(A) motions from Down to one-Up. Reduced interactions between RBD(A) and RBD(B) in one-Up induce RBD(B) motions toward two-Up. The simulations overall agree with cryo-electron microscopy structure distributions and FRET experiments and provide hidden functional structures, namely, intermediates along Down-to-one-Up transition with druggable cryptic pockets as well as one-Open with a maximum exposed RBD. The inherent flexibility of S-protein thus provides essential information for antiviral drug rational design or vaccine development. |*Spike Glycoprotein, Coronavirus/chemistry[MESH] |COVID-19[MESH] |Cryoelectron Microscopy[MESH] |Humans[MESH] |Protein Domains[MESH]The inherent flexibility of receptor binding domains in SARS-CoV-2 spi(epmc).pdf DeepDyve Pubget Overpricing