HAL will be down for maintenance from Friday, June 10 at 4pm through Monday, June 13 at 9am. More information
Skip to Main content Skip to Navigation
Journal articles

Flexibility and mobility of SARS-CoV-2-related protein structures

Abstract : Abstract The worldwide CoVid-19 pandemic has led to an unprecedented push across the whole of the scientific community to develop a potent antiviral drug and vaccine as soon as possible. Existing academic, governmental and industrial institutions and companies have engaged in large-scale screening of existing drugs, in vitro, in vivo and in silico. Here, we are using in silico modelling of possible SARS-CoV-2 drug targets, as deposited on the Protein Databank (PDB), and ascertain their dynamics, flexibility and rigidity. For example, for the SARS-CoV-2 spike protein—using its complete homo-trimer configuration with 2905 residues—our method identifies a large-scale opening and closing of the S1 subunit through movement of the S $${}^\text{B}$$ B domain. We compute the full structural information of this process, allowing for docking studies with possible drug structures. In a dedicated database, we present similarly detailed results for the further, nearly 300, thus far resolved SARS-CoV-2-related protein structures in the PDB.
Document type :
Journal articles
Complete list of metadata

https://hal-cnrs.archives-ouvertes.fr/hal-03636461
Contributor : Rudo Roemer Connect in order to contact the contributor
Submitted on : Sunday, April 10, 2022 - 2:37:21 PM
Last modification on : Saturday, April 16, 2022 - 3:35:40 AM

File

2020.07.12.199364v1.full.pdf
Files produced by the author(s)

Identifiers

Collections

Citation

Rudolf Römer, Navodya Römer, A. Katrine Wallis. Flexibility and mobility of SARS-CoV-2-related protein structures. Scientific Reports, Nature Publishing Group, 2021, 11 (1), pp.4257. ⟨10.1038/s41598-021-82849-2⟩. ⟨hal-03636461⟩

Share

Metrics

Record views

11

Files downloads

11