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10.1038/s41586-020-2179-y http://scihub22266oqcxt.onion/10.1038/s41586-020-2179-y 32225175!7328981!32225175     free     free     free Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\32225175.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117       Nature 2020 ; 581 (7807): 221-224 Nephropedia Template TP {{tp|p=32225175|t=2020. Structural basis of receptor recognition by SARS-CoV-2 |pdf=|usr=}}{{32225175}} gab.com Text Structural basis of receptor recognition by SARS-CoV-2 JO: Nature http://www.kidney.de/pget.php?&tw=1&pmid=32225175 #FOAvip A novel severe acute respiratory syndrome (SARS)-like coronavirus (SARS-CoV-2) recently emerged and is rapidly spreading in humans, causing COVID-19(1,2). A key to tackling this pandemic is to understand the receptor recognition mechanism of the virus, which regulates its infectivity, pathogenesis and host range. SARS-CoV-2 and SARS-CoV recognize the same receptor-angiotensin-converting enzyme 2 (ACE2)-in humans(3,4). Here we determined the crystal structure of the receptor-binding domain (RBD) of the spike protein of SARS-CoV-2 (engineered to facilitate crystallization) in complex with ACE2. In comparison with the SARS-CoV RBD, an ACE2-binding ridge in SARS-CoV-2 RBD has a more compact conformation; moreover, several residue changes in the SARS-CoV-2 RBD stabilize two virus-binding hotspots at the RBD-ACE2 interface. These structural features of SARS-CoV-2 RBD increase its ACE2-binding affinity. Additionally, we show that RaTG13, a bat coronavirus that is closely related to SARS-CoV-2, also uses human ACE2 as its receptor. The differences among SARS-CoV-2, SARS-CoV and RaTG13 in ACE2 recognition shed light on the potential animal-to-human transmission of SARS-CoV-2. This study provides guidance for intervention strategies that target receptor recognition by SARS-CoV-2. Twit Text FOAVip Structural basis of receptor recognition by SARS-CoV-2 ????Nature http://www.kidney.de/pget.php?&tw=1&pmid=32225175 #FOAvip Twit Text # Free Paper on # # # # # LINK http://www.kidney.de/pget.php?&tw=1&pmid=32225175 #FOAvip English Wikipedia <ref>{{Cite pmid|32225175}}</ref> Structural basis of receptor recognition by SARS-CoV-2 #MMPMID32225175 Shang J; Ye G; Shi K; Wan Y; Luo C; Aihara H; Geng Q; Auerbach A; Li F Nature 2020[May]; 581 (7807): 221-224 PMID32225175show ga A novel severe acute respiratory syndrome (SARS)-like coronavirus (SARS-CoV-2) recently emerged and is rapidly spreading in humans, causing COVID-19(1,2). A key to tackling this pandemic is to understand the receptor recognition mechanism of the virus, which regulates its infectivity, pathogenesis and host range. SARS-CoV-2 and SARS-CoV recognize the same receptor-angiotensin-converting enzyme 2 (ACE2)-in humans(3,4). Here we determined the crystal structure of the receptor-binding domain (RBD) of the spike protein of SARS-CoV-2 (engineered to facilitate crystallization) in complex with ACE2. In comparison with the SARS-CoV RBD, an ACE2-binding ridge in SARS-CoV-2 RBD has a more compact conformation; moreover, several residue changes in the SARS-CoV-2 RBD stabilize two virus-binding hotspots at the RBD-ACE2 interface. These structural features of SARS-CoV-2 RBD increase its ACE2-binding affinity. Additionally, we show that RaTG13, a bat coronavirus that is closely related to SARS-CoV-2, also uses human ACE2 as its receptor. The differences among SARS-CoV-2, SARS-CoV and RaTG13 in ACE2 recognition shed light on the potential animal-to-human transmission of SARS-CoV-2. This study provides guidance for intervention strategies that target receptor recognition by SARS-CoV-2. |Angiotensin-Converting Enzyme 2[MESH] |Animals[MESH] |Betacoronavirus/*chemistry/drug effects/metabolism[MESH] |Binding Sites[MESH] |COVID-19[MESH] |China/epidemiology[MESH] |Chiroptera/virology[MESH] |Coronavirus Infections/drug therapy/epidemiology/transmission/virology[MESH] |Coronavirus/chemistry/isolation & purification[MESH] |Crystallization[MESH] |Crystallography, X-Ray[MESH] |Disease Reservoirs/virology[MESH] |Eutheria/virology[MESH] |Humans[MESH] |Models, Molecular[MESH] |Pandemics[MESH] |Peptidyl-Dipeptidase A/*chemistry/*metabolism[MESH] |Pneumonia, Viral/drug therapy/epidemiology/transmission/virology[MESH] |Protein Binding[MESH] |Protein Domains[MESH] |Protein Stability[MESH] |Receptors, Virus/*chemistry/*metabolism[MESH] |SARS-CoV-2[MESH] |Severe acute respiratory syndrome-related coronavirus/chemistry[MESH] |Spike Glycoprotein, Coronavirus/*chemistry/genetics/*metabolism[MESH]Structural basis of receptor recognition by SARS-CoV-2 (epmc).pdf DeepDyve Pubget Overpricing