Identifying promising druggable binding sites and their flexibility to target the receptor-binding domain of SARS-CoV-2 spike protein

• Published in: Computational and structural biotechnology journal Vol. 21; pp. 2339 - 2351
• Main Authors: Ghoula, M., Naceri, S., Sitruk, S., Flatters, D., Moroy, G., Camproux, A.C.
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.01.2023; Published by Elsevier B.V. on behalf of Research Network of Computational and Structural Biotechnology; Elsevier
• Subjects: Binding site flexibility; biotechnology; COVID-19 variants; domain; Druggable binding sites; Hot spot residues; humans; Key-residues; molecular dynamics; Molecular dynamics simulation; mutation; peptidyl-dipeptidase A; Pocket tracking; prediction; SARS-CoV-2; Severe acute respiratory syndrome coronavirus 2; Spike protein; Structural flexibility; viruses; Pocket tracking; SARS-CoV-2; Spike protein; Binding site flexibility; Key-residues; COVID-19 variants; Structural flexibility; Molecular dynamics simulation; Druggable binding sites; Hot spot residues

The spike protein of severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) is crucial for viral infection. The interaction of its receptor-binding domain (RBD) with the human angiotensin-converting enzyme 2 (ACE2) protein is required for the virus to enter the host cell. We identified RBD bin...