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10.1038/s41586-020-2179-y

http://scihub22266oqcxt.onion/10.1038/s41586-020-2179-y
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32225175!7328981!32225175
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suck abstract from ncbi

pmid32225175      Nature 2020 ; 581 (7807): 221-224
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  • 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]


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