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TitleStructure and binding properties of Pangolin-CoV spike glycoprotein inform the evolution of SARS-CoV-2.
Journal, issue, pagesNat Commun, Vol. 12, Issue 1, Page 837, Year 2021
Publish dateFeb 5, 2021
AuthorsAntoni G Wrobel / Donald J Benton / Pengqi Xu / Lesley J Calder / Annabel Borg / Chloë Roustan / Stephen R Martin / Peter B Rosenthal / John J Skehel / Steven J Gamblin /
PubMed AbstractCoronaviruses of bats and pangolins have been implicated in the origin and evolution of the pandemic SARS-CoV-2. We show that spikes from Guangdong Pangolin-CoVs, closely related to SARS-CoV-2, bind ...Coronaviruses of bats and pangolins have been implicated in the origin and evolution of the pandemic SARS-CoV-2. We show that spikes from Guangdong Pangolin-CoVs, closely related to SARS-CoV-2, bind strongly to human and pangolin ACE2 receptors. We also report the cryo-EM structure of a Pangolin-CoV spike protein and show it adopts a fully-closed conformation and that, aside from the Receptor-Binding Domain, it resembles the spike of a bat coronavirus RaTG13 more than that of SARS-CoV-2.
External linksNat Commun / PubMed:33547281 / PubMed Central
MethodsEM (single particle)
Resolution2.9 Å
Structure data

12130

7bbh

EMDB-12130, PDB-7bbh:
Structure of Coronavirus Spike from Smuggled Guangdong Pangolin
Method: EM (single particle) / Resolution: 2.9 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

Source
  • pangolin coronavirus
KeywordsVIRAL PROTEIN / Coronavirus / Pangolin / Spike / Smuggled / DSP

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