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10.1126/science.abb7269 http://scihub22266oqcxt.onion/10.1126/science.abb7269 32245784!7164391!32245784     free     free     free Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534 Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534       Science 2020 ; 368 (6491): 630-633 Nephropedia Template TP {{tp|p=32245784|t=2020. A highly conserved cryptic epitope in the receptor binding domains of SARS-CoV-2 and SARS-CoV |pdf=|usr=}}{{32245784}} gab.com Text A highly conserved cryptic epitope in the receptor binding domains of SARS-CoV-2 and SARS-CoV JO: Science http://www.kidney.de/pget.php?&tw=1&pmid=32245784 #FOAvip The outbreak of coronavirus disease 2019 (COVID-19) caused by severe acute respiratory syndrome-coronavirus 2 (SARS-CoV-2) has now become a pandemic, but there is currently very little understanding of the antigenicity of the virus. We therefore determined the crystal structure of CR3022, a neutralizing antibody previously isolated from a convalescent SARS patient, in complex with the receptor binding domain (RBD) of the SARS-CoV-2 spike (S) protein at 3.1-angstrom resolution. CR3022 targets a highly conserved epitope, distal from the receptor binding site, that enables cross-reactive binding between SARS-CoV-2 and SARS-CoV. Structural modeling further demonstrates that the binding epitope can only be accessed by CR3022 when at least two RBDs on the trimeric S protein are in the "up" conformation and slightly rotated. These results provide molecular insights into antibody recognition of SARS-CoV-2. Twit Text FOAVip A highly conserved cryptic epitope in the receptor binding domains of SARS-CoV-2 and SARS-CoV ????Science http://www.kidney.de/pget.php?&tw=1&pmid=32245784 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32245784 #FOAvip English Wikipedia <ref>{{Cite pmid|32245784}}</ref> A highly conserved cryptic epitope in the receptor binding domains of SARS-CoV-2 and SARS-CoV #MMPMID32245784 Yuan M; Wu NC; Zhu X; Lee CD; So RTY; Lv H; Mok CKP; Wilson IA Science 2020[May]; 368 (6491): 630-633 PMID32245784show ga The outbreak of coronavirus disease 2019 (COVID-19) caused by severe acute respiratory syndrome-coronavirus 2 (SARS-CoV-2) has now become a pandemic, but there is currently very little understanding of the antigenicity of the virus. We therefore determined the crystal structure of CR3022, a neutralizing antibody previously isolated from a convalescent SARS patient, in complex with the receptor binding domain (RBD) of the SARS-CoV-2 spike (S) protein at 3.1-angstrom resolution. CR3022 targets a highly conserved epitope, distal from the receptor binding site, that enables cross-reactive binding between SARS-CoV-2 and SARS-CoV. Structural modeling further demonstrates that the binding epitope can only be accessed by CR3022 when at least two RBDs on the trimeric S protein are in the "up" conformation and slightly rotated. These results provide molecular insights into antibody recognition of SARS-CoV-2. |*Epitopes/chemistry/immunology[MESH] |Amino Acid Sequence[MESH] |Angiotensin-Converting Enzyme 2[MESH] |Antibodies, Neutralizing/chemistry/immunology[MESH] |Antibodies, Viral/chemistry/immunology[MESH] |Antibody Affinity[MESH] |Antigens, Viral/chemistry/immunology[MESH] |Betacoronavirus/*chemistry/*immunology[MESH] |Binding Sites[MESH] |Cross Reactions[MESH] |Crystallography, X-Ray[MESH] |Models, Molecular[MESH] |Peptidyl-Dipeptidase A/chemistry/metabolism[MESH] |Protein Conformation[MESH] |Protein Domains[MESH] |Protein Interaction Domains and Motifs/immunology[MESH] |Receptors, Coronavirus[MESH] |Receptors, Virus/chemistry/metabolism[MESH] |SARS-CoV-2[MESH] |Severe acute respiratory syndrome-related coronavirus/*chemistry/*immunology[MESH]A highly conserved cryptic epitope in the receptor binding domains of (epmc).pdf DeepDyve Pubget Overpricing