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http://purl.uniprot.org/citations/34385690http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/34385690http://www.w3.org/2000/01/rdf-schema#comment"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 π-π 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."xsd:string
http://purl.uniprot.org/citations/34385690http://purl.org/dc/terms/identifier"doi:10.1038/s41594-021-00652-z"xsd:string
http://purl.uniprot.org/citations/34385690http://purl.uniprot.org/core/author"Wu H.C."xsd:string
http://purl.uniprot.org/citations/34385690http://purl.uniprot.org/core/author"Chang Y.C."xsd:string
http://purl.uniprot.org/citations/34385690http://purl.uniprot.org/core/author"Ho M.R."xsd:string
http://purl.uniprot.org/citations/34385690http://purl.uniprot.org/core/author"Yang T.J."xsd:string
http://purl.uniprot.org/citations/34385690http://purl.uniprot.org/core/author"Chen W.Y."xsd:string
http://purl.uniprot.org/citations/34385690http://purl.uniprot.org/core/author"Lin H.T."xsd:string
http://purl.uniprot.org/citations/34385690http://purl.uniprot.org/core/author"Liang K.H."xsd:string
http://purl.uniprot.org/citations/34385690http://purl.uniprot.org/core/author"Hsu S.D."xsd:string
http://purl.uniprot.org/citations/34385690http://purl.uniprot.org/core/author"Yu P.Y."xsd:string
http://purl.uniprot.org/citations/34385690http://purl.uniprot.org/core/author"Tso H.C."xsd:string
http://purl.uniprot.org/citations/34385690http://purl.uniprot.org/core/date"2021"xsd:gYear
http://purl.uniprot.org/citations/34385690http://purl.uniprot.org/core/name"Nat Struct Mol Biol"xsd:string
http://purl.uniprot.org/citations/34385690http://purl.uniprot.org/core/pages"731-739"xsd:string
http://purl.uniprot.org/citations/34385690http://purl.uniprot.org/core/title"Effect of SARS-CoV-2 B.1.1.7 mutations on spike protein structure and function."xsd:string
http://purl.uniprot.org/citations/34385690http://purl.uniprot.org/core/volume"28"xsd:string
http://purl.uniprot.org/citations/34385690http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/34385690
http://purl.uniprot.org/citations/34385690http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/34385690
http://purl.uniprot.org/uniprot/P0DTC2#attribution-653553298726AB2317AF88396E18E8E9http://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/34385690
http://purl.uniprot.org/uniprot/#_P42212-mappedCitation-34385690http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/34385690
http://purl.uniprot.org/uniprot/#_P0DTC2-mappedCitation-34385690http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/34385690
http://purl.uniprot.org/uniprot/#_Q9BYF1-mappedCitation-34385690http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/34385690
http://purl.uniprot.org/uniprot/Q9BYF1http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/34385690