A New Crystal Form of the SARS-CoV-2 Receptor Binding Domain: CR3022 Complex—An Ideal Target for In-Crystal Fragment Screening of the ACE2 Binding Site Surface

Charlie Nichols; Joseph Ng; Annika Keshu; Franca Fraternali; Gian F. De Nicola

doi:10.3389/fphar.2020.615211

A New Crystal Form of the SARS-CoV-2 Receptor Binding Domain: CR3022 Complex—An Ideal Target for In-Crystal Fragment Screening of the ACE2 Binding Site Surface

Charlie Nichols, Joseph Ng, Annika Keshu, Franca Fraternali, Gian F. De Nicola^*

^*Corresponding author for this work

Research output: Contribution to journal › Article › peer-review

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Abstract

In-crystal fragment screening is a powerful tool to chemically probe the surfaces used by proteins to interact, and identify the chemical space worth exploring to design protein-protein inhibitors. A crucial prerequisite is the identification of a crystal form where the target area is exposed and accessible to be probed by fragments. Here we report a crystal form of the SARS-CoV-2 Receptor Binding Domain in complex with the CR3022 antibody where the ACE2 binding site on the Receptor Binding Domain is exposed and accessible. This crystal form of the complex is a valuable tool to develop antiviral molecules that could act by blocking the virus entry in cells.

Original language	English
Article number	615211
Journal	Frontiers in Pharmacology
Volume	11
DOIs	https://doi.org/10.3389/fphar.2020.615211
Publication status	Published - 14 Dec 2020

Keywords

CR3022
drug discovery
in-crystal fragment screening
PPI inhibitors
SARC-CoV-2-RBD

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

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10.3389/fphar.2020.615211

A New Crystal Form of the SARS-CoV-2 Receptor Binding Domain: CR3022 Complex—An Ideal Target for In-Crystal Fragment Screening of the ACE2 Binding Site SurfaceFinal published version, 864 KBLicence: CC BY

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abstract = "In-crystal fragment screening is a powerful tool to chemically probe the surfaces used by proteins to interact, and identify the chemical space worth exploring to design protein-protein inhibitors. A crucial prerequisite is the identification of a crystal form where the target area is exposed and accessible to be probed by fragments. Here we report a crystal form of the SARS-CoV-2 Receptor Binding Domain in complex with the CR3022 antibody where the ACE2 binding site on the Receptor Binding Domain is exposed and accessible. This crystal form of the complex is a valuable tool to develop antiviral molecules that could act by blocking the virus entry in cells.",

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AU - Ng, Joseph

AU - Keshu, Annika

AU - Fraternali, Franca

AU - De Nicola, Gian F.

PY - 2020/12/14

Y1 - 2020/12/14

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AB - In-crystal fragment screening is a powerful tool to chemically probe the surfaces used by proteins to interact, and identify the chemical space worth exploring to design protein-protein inhibitors. A crucial prerequisite is the identification of a crystal form where the target area is exposed and accessible to be probed by fragments. Here we report a crystal form of the SARS-CoV-2 Receptor Binding Domain in complex with the CR3022 antibody where the ACE2 binding site on the Receptor Binding Domain is exposed and accessible. This crystal form of the complex is a valuable tool to develop antiviral molecules that could act by blocking the virus entry in cells.

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KW - drug discovery

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A New Crystal Form of the SARS-CoV-2 Receptor Binding Domain: CR3022 Complex—An Ideal Target for In-Crystal Fragment Screening of the ACE2 Binding Site Surface

Abstract

Keywords

UN SDGs

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