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10.1038/s41586-020-2180-5 http://scihub22266oqcxt.onion/10.1038/s41586-020-2180-5 32225176!ä!32225176 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 235.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Nature 2020 ; 581 (7807): 215-220 Nephropedia Template TP {{tp|p=32225176|t=2020. Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor |pdf=|usr=}}{{32225176}} gab.com Text Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor JO: Nature http://www.kidney.de/pget.php?&tw=1&pmid=32225176 #FOAvip A new and highly pathogenic coronavirus (severe acute respiratory syndrome coronavirus-2, SARS-CoV-2) caused an outbreak in Wuhan city, Hubei province, China, starting from December 2019 that quickly spread nationwide and to other countries around the world(1-3). Here, to better understand the initial step of infection at an atomic level, we determined the crystal structure of the receptor-binding domain (RBD) of the spike protein of SARS-CoV-2 bound to the cell receptor ACE2. The overall ACE2-binding mode of the SARS-CoV-2 RBD is nearly identical to that of the SARS-CoV RBD, which also uses ACE2 as the cell receptor(4). Structural analysis identified residues in the SARS-CoV-2 RBD that are essential for ACE2 binding, the majority of which either are highly conserved or share similar side chain properties with those in the SARS-CoV RBD. Such similarity in structure and sequence strongly indicate convergent evolution between the SARS-CoV-2 and SARS-CoV RBDs for improved binding to ACE2, although SARS-CoV-2 does not cluster within SARS and SARS-related coronaviruses(1-3,5). The epitopes of two SARS-CoV antibodies that target the RBD are also analysed for binding to the SARS-CoV-2 RBD, providing insights into the future identification of cross-reactive antibodies. Twit Text FOAVip Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor ????Nature http://www.kidney.de/pget.php?&tw=1&pmid=32225176 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32225176 #FOAvip English Wikipedia <ref>{{Cite pmid|32225176}}</ref> Structure of the SARS-CoV-2 spike receptor-binding domain bound to the ACE2 receptor #MMPMID32225176 Lan J; Ge J; Yu J; Shan S; Zhou H; Fan S; Zhang Q; Shi X; Wang Q; Zhang L; Wang X Nature 2020[May]; 581 (7807): 215-220 PMID32225176show ga A new and highly pathogenic coronavirus (severe acute respiratory syndrome coronavirus-2, SARS-CoV-2) caused an outbreak in Wuhan city, Hubei province, China, starting from December 2019 that quickly spread nationwide and to other countries around the world(1-3). Here, to better understand the initial step of infection at an atomic level, we determined the crystal structure of the receptor-binding domain (RBD) of the spike protein of SARS-CoV-2 bound to the cell receptor ACE2. The overall ACE2-binding mode of the SARS-CoV-2 RBD is nearly identical to that of the SARS-CoV RBD, which also uses ACE2 as the cell receptor(4). Structural analysis identified residues in the SARS-CoV-2 RBD that are essential for ACE2 binding, the majority of which either are highly conserved or share similar side chain properties with those in the SARS-CoV RBD. Such similarity in structure and sequence strongly indicate convergent evolution between the SARS-CoV-2 and SARS-CoV RBDs for improved binding to ACE2, although SARS-CoV-2 does not cluster within SARS and SARS-related coronaviruses(1-3,5). The epitopes of two SARS-CoV antibodies that target the RBD are also analysed for binding to the SARS-CoV-2 RBD, providing insights into the future identification of cross-reactive antibodies. |Amino Acid Sequence[MESH] |Angiotensin-Converting Enzyme 2[MESH] |Antibodies, Neutralizing/immunology[MESH] |Betacoronavirus/*chemistry/metabolism[MESH] |Binding Sites[MESH] |Conserved Sequence[MESH] |Crystallography, X-Ray[MESH] |Epitopes/chemistry/immunology[MESH] |Evolution, Molecular[MESH] |Humans[MESH] |Hydrogen Bonding[MESH] |Models, Molecular[MESH] |Peptidyl-Dipeptidase A/*chemistry/*metabolism[MESH] |Protein Binding[MESH] |Protein Domains[MESH] |Receptors, Virus/*chemistry/*metabolism[MESH] |SARS-CoV-2[MESH] |Salts/chemistry[MESH] |Sequence Alignment[MESH] |Severe acute respiratory syndrome-related coronavirus/chemistry[MESH] |Spike Glycoprotein, Coronavirus/*chemistry/*metabolism[MESH]Structure of the SARS-CoV-2 spike receptor-binding domain bound to the(epmc).pdf DeepDyve Pubget Overpricing