Flexibility and mobility of SARS-CoV-2-related protein structures - Archive ouverte HAL Access content directly
Journal Articles Scientific Reports Year : 2021

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

(1, 2) , (3) , (4)
1
2
3
4
Rudolf Römer
Navodya Römer
• Function : Author
A. Katrine Wallis

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.

Dates and versions

hal-03636461 , version 1 (10-04-2022)

Identifiers

• HAL Id : hal-03636461 , version 1
• DOI :
• PUBMEDCENTRAL :

Cite

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

30 View