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10.1126/science.abd5223 http://scihub22266oqcxt.onion/10.1126/science.abd5223 32817270!7665311!32817270     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 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 Deprecated: Implicit conversion from float 231.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Science 2020 ; 370 (6513): 203-208 Nephropedia Template TP {{tp|p=32817270|t=2020. In situ structural analysis of SARS-CoV-2 spike reveals flexibility mediated by three hinges |pdf=|usr=}}{{32817270}} gab.com Text In situ structural analysis of SARS-CoV-2 spike reveals flexibility mediated by three hinges JO: Science http://www.kidney.de/pget.php?&tw=1&pmid=32817270 #FOAvip The spike protein (S) of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is required for cell entry and is the primary focus for vaccine development. In this study, we combined cryo-electron tomography, subtomogram averaging, and molecular dynamics simulations to structurally analyze S in situ. Compared with the recombinant S, the viral S was more heavily glycosylated and occurred mostly in the closed prefusion conformation. We show that the stalk domain of S contains three hinges, giving the head unexpected orientational freedom. We propose that the hinges allow S to scan the host cell surface, shielded from antibodies by an extensive glycan coat. The structure of native S contributes to our understanding of SARS-CoV-2 infection and potentially to the development of safe vaccines. Twit Text FOAVip In situ structural analysis of SARS-CoV-2 spike reveals flexibility mediated by three hinges ????Science http://www.kidney.de/pget.php?&tw=1&pmid=32817270 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32817270 #FOAvip English Wikipedia <ref>{{Cite pmid|32817270}}</ref> In situ structural analysis of SARS-CoV-2 spike reveals flexibility mediated by three hinges #MMPMID32817270 Turonova B; Sikora M; Schurmann C; Hagen WJH; Welsch S; Blanc FEC; von Bulow S; Gecht M; Bagola K; Horner C; van Zandbergen G; Landry J; de Azevedo NTD; Mosalaganti S; Schwarz A; Covino R; Muhlebach MD; Hummer G; Krijnse Locker J; Beck M Science 2020[Oct]; 370 (6513): 203-208 PMID32817270show ga The spike protein (S) of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is required for cell entry and is the primary focus for vaccine development. In this study, we combined cryo-electron tomography, subtomogram averaging, and molecular dynamics simulations to structurally analyze S in situ. Compared with the recombinant S, the viral S was more heavily glycosylated and occurred mostly in the closed prefusion conformation. We show that the stalk domain of S contains three hinges, giving the head unexpected orientational freedom. We propose that the hinges allow S to scan the host cell surface, shielded from antibodies by an extensive glycan coat. The structure of native S contributes to our understanding of SARS-CoV-2 infection and potentially to the development of safe vaccines. |*Molecular Dynamics Simulation[MESH] |Betacoronavirus/*chemistry[MESH] |Cryoelectron Microscopy[MESH] |Electron Microscope Tomography[MESH] |Glycosylation[MESH] |Humans[MESH] |Protein Domains[MESH] |Protein Multimerization[MESH] |SARS-CoV-2[MESH]In situ structural analysis of SARS-CoV-2 spike reveals flexibility me(epmc).pdf DeepDyve Pubget Overpricing