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TitleAnalysis of SARS-CoV-2 variant mutations reveals neutralization escape mechanisms and the ability to use ACE2 receptors from additional species.
Journal, issue, pagesImmunity, Vol. 54, Page 1611-1621.e5, Year 2021
Publish dateMar 2, 2021 (structure data deposition date)
AuthorsWang, R. / Zhang, Q. / Ge, J. / Ren, W. / Zhang, R. / Lan, J. / Ju, B. / Su, B. / Yu, F. / Chen, P. ...Wang, R. / Zhang, Q. / Ge, J. / Ren, W. / Zhang, R. / Lan, J. / Ju, B. / Su, B. / Yu, F. / Chen, P. / Liao, H. / Feng, Y. / Li, X. / Shi, X. / Zhang, Z. / Zhang, F. / Ding, Q. / Zhang, T. / Wang, X. / Zhang, L.
External linksImmunity / PubMed:34166623
MethodsX-ray diffraction
Resolution2.09 Å
Structure data

PDB-7e8m:
Crystal structure of SARS-CoV-2 antibody P2C-1F11 with mutated RBD
Method: X-RAY DIFFRACTION / Resolution: 2.09 Å

Chemicals

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

ChemComp-HOH:
WATER

Source
  • severe acute respiratory syndrome coronavirus 2
  • homo sapiens (human)
KeywordsVIRAL PROTEIN/IMMUNE SYSTEM / SARS-CoV-2 spike / receptor binding domain / antibody / VIRAL PROTEIN / VIRAL PROTEIN-IMMUNE SYSTEM complex

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