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ISSN / EISSN : 01934511 / 10959203
Total articles ≅ 270,237
Google Scholar h5-index: 345
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Meng Yuan, Nicholas C. Wu, Xueyong Zhu, Chang-Chun David Lee, Ray T. Y. So, Huibin Lv, Chris K. P. Mok, Ian A. Wilson
Science; doi:10.1126/science.abb7269

Abstract:
The outbreak of COVID-19 caused by SARS-CoV-2 virus has now become a pandemic, but there is currently very little understanding of the antigenicity of the virus. We therefore determined the crystal structure of CR3022, a neutralizing antibody previously isolated from a convalescent SARS patient, in complex with the receptor-binding domain (RBD) of the SARS-CoV-2 spike (S) protein to 3.1 Å. CR3022 targets a highly conserved epitope, distal from the receptor-binding site, that enables cross-reactive binding between SARS-CoV-2 and SARS-CoV. Structural modeling further demonstrates that the binding epitope can only be accessed by CR3022 when at least two RBD on the trimeric S protein are in the "up" conformation and slightly rotated. Overall, this study provides molecular insights into antibody recognition of SARS-CoV-2.
Elizabeth Pennisi
Science; doi:10.1126/science.abc0608

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Jeffrey Mervis
Science; doi:10.1126/science.abc0649

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Vineeth Venugopal
Science; doi:10.1126/science.abc0657

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Mingwei Min, Yao Rong, Chengzhe Tian, Sabrina Spencer
Science; doi:10.1126/science.aay8241

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Andrew M. Sugden
Science, Volume 368, pp 42.11-44; doi:10.1126/science.368.6486.42-k

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Mark Miodownik
Science, Volume 368, pp 41-41; doi:10.1126/science.aba8965

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Meredith Wadman
Science, Volume 368, pp 21-25; doi:10.1126/science.368.6486.21

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Pamela J. Hines
Science, Volume 368, pp 42.12-44; doi:10.1126/science.368.6486.42-l

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Jake Yeston
Science, Volume 368, pp 43.6-44; doi:10.1126/science.368.6486.43-f

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