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10.1038/s41594-021-00652-z

http://scihub22266oqcxt.onion/10.1038/s41594-021-00652-z
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34385690!ä!34385690

suck abstract from ncbi


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pmid34385690      Nat+Struct+Mol+Biol 2021 ; 28 (9): 731-739
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  • Effect of SARS-CoV-2 B 1 1 7 mutations on spike protein structure and function #MMPMID34385690
  • Yang TJ; Yu PY; Chang YC; Liang KH; Tso HC; Ho MR; Chen WY; Lin HT; Wu HC; Hsu SD
  • Nat Struct Mol Biol 2021[Sep]; 28 (9): 731-739 PMID34385690show ga
  • The B.1.1.7 variant of SARS-CoV-2 first detected in the UK harbors amino-acid substitutions and deletions in the spike protein that potentially enhance host angiotensin conversion enzyme 2 (ACE2) receptor binding and viral immune evasion. Here we report cryo-EM structures of the spike protein of B.1.1.7 in the apo and ACE2-bound forms. The apo form showed one or two receptor-binding domains (RBDs) in the open conformation, without populating the fully closed state. All three RBDs were engaged in ACE2 binding. The B.1.1.7-specific A570D mutation introduces a molecular switch that could modulate the opening and closing of the RBD. The N501Y mutation introduces a pi-pi interaction that enhances RBD binding to ACE2 and abolishes binding of a potent neutralizing antibody (nAb). Cryo-EM also revealed how a cocktail of two nAbs simultaneously bind to all three RBDs, and demonstrated the potency of the nAb cocktail to neutralize different SARS-CoV-2 pseudovirus strains, including B.1.1.7.
  • |*Mutation[MESH]
  • |Angiotensin-Converting Enzyme 2/chemistry/metabolism[MESH]
  • |Antibodies, Neutralizing/immunology[MESH]
  • |Antibodies, Viral/immunology[MESH]
  • |Binding Sites/genetics[MESH]
  • |COVID-19/metabolism/*prevention & control/virology[MESH]
  • |Cryoelectron Microscopy[MESH]
  • |Humans[MESH]
  • |Models, Molecular[MESH]
  • |Protein Binding[MESH]
  • |Protein Domains[MESH]
  • |Receptors, Virus/chemistry/metabolism[MESH]
  • |SARS-CoV-2/*genetics/immunology/physiology[MESH]


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