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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

DOI: 10.3389/fphar.2020.615211 DOI Help

Authors: Charlie Nichols (Rayne Institute, St Thomas’ Hospital, King’s College London; The Randall Centre for Cell and Molecular Biophysics, King’s College London) , Joseph Ng (Rayne Institute, St Thomas’ Hospital, King’s College London) , Annika Keshu (Rayne Institute, St Thomas’ Hospital, King’s College London) , Franca Fraternali (Rayne Institute, St Thomas’ Hospital, King’s College London) , Gian F. De Nicola (Rayne Institute, St Thomas’ Hospital, King’s College London; The Randall Centre for Cell and Molecular Biophysics, King’s College London)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Frontiers In Pharmacology , VOL 11

State: Published (Approved)
Published: December 2020
Diamond Proposal Number(s): 27049

Open Access Open Access

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.

Diamond Keywords: COVID-19; Viruses

Subject Areas: Biology and Bio-materials, Medicine, Chemistry


Instruments: I24-Microfocus Macromolecular Crystallography

Added On: 04/01/2021 11:38

Documents:
fphar-11-615211.pdf

Discipline Tags:

Life Sciences & Biotech Health & Wellbeing Drug Discovery Infectious Diseases Pathogens Structural biology Chemistry Biochemistry

Technical Tags:

Diffraction Macromolecular Crystallography (MX)