Author: M. Gordon Joyce; Rajeshwer S. Sankhala; Wei-Hung Chen; Misook Choe; Hongjun Bai; Agnes Hajduczki; Lianying Yan; Spencer L. Sterling; Caroline E. Peterson; Ethan C. Green; Clayton Smith; Natalia de Val; Mihret Amare; Paul Scott; Eric D. Laing; Christopher C. Broder; Morgane Rolland; Nelson L. Michael; Kayvon Modjarrad
Title: A Cryptic Site of Vulnerability on the Receptor Binding Domain of the SARS-CoV-2 Spike Glycoprotein Document date: 2020_3_17
ID: ebbzx8yr_20
Snippet: author/funder. This article is a US Government work. It is not subject to copyright under 17 USC 105 and is also made available for use under The copyright holder for this preprint (which was not peer-reviewed) is the . https://doi.org/10.1101/2020.03.15.992883 doi: bioRxiv preprint Figure 4 . Identification of CR3022 epitope as a "cryptic" epitope. Structural alignment of the SARS-CoV-2 RBD-CR3022 complex with the SARS-CoV S-2P structure. A The .....
Document: author/funder. This article is a US Government work. It is not subject to copyright under 17 USC 105 and is also made available for use under The copyright holder for this preprint (which was not peer-reviewed) is the . https://doi.org/10.1101/2020.03.15.992883 doi: bioRxiv preprint Figure 4 . Identification of CR3022 epitope as a "cryptic" epitope. Structural alignment of the SARS-CoV-2 RBD-CR3022 complex with the SARS-CoV S-2P structure. A The RBD-CR3022 structure is aligned to the SARS-CoV trimer structure (surface representation; PDB ID: 6CS1), where two RBD molecules are located in the "up" conformation. In this static structure, the Fc1 region of CR3022 (ribbon representation) clashes with the NTD of the same protomer. However, the epitope is fully accessible when more than one RBD is in the "up" representation. B Biolayer interferometry measurement of CR3022 binding to SARS S proteins with trypsin treatment or ACE2 receptor binding. C CR3022 binding to a serial dilution of SARS S-2P protein following trypsin treatment. a CC0 license.
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