SARS-CoV-2 Spike receptor-binding domain with a G485R mutation in complex with human ACE2
Weekley, C. M.; Purcell, D. F. J.; Parker, M. W.
Show abstract
Since SARS-CoV-2 emerged in 2019, genomic sequencing has identified mutations in the viral RNA including in the receptor-binding domain of the Spike protein. Structural characterisation of the Spike carrying point mutations aids in our understanding of how these mutations impact binding of the protein to its human receptor, ACE2, and to therapeutic antibodies. The Spike G485R mutation has been observed in multiple isolates of the virus and mutation of the adjacent residue E484 to lysine is known to contribute to antigenic escape. Here, we have crystallised the SARS-CoV-2 Spike receptor-binding domain with a G485R mutation in complex with human ACE2. The crystal structure shows that while the G485 residue does not have a direct interaction with ACE2, its mutation to arginine affects the structure of the loop made by residues 480-488 in the receptor-binding motif, disrupting the interactions of neighbouring residues with ACE2 and with potential implications for antigenic escape from vaccines, antibodies and other biologics directed against SARS-CoV-2 Spike.
Matching journals
The top 5 journals account for 50% of the predicted probability mass.
Similar papers in this journal
- Nanobodies identify an activated state of the TRIB2 pseudokinase 93%
- Structure and dynamic association of an assembly platform subcomplex of the bacterial type II secretion system 93%
- A common binding motif in the ET domain of BRD3 forms polymorphic structural interfaces with host and viral proteins 93%
Similar papers in this journal
- Thrombospondin module 1 domain (TSP1) of the matricellular protein CCN3 shows an atypical disulfide pattern and incomplete CWR layers 94%
- Possible Implications of AlphaFold2 for Crystallographic Phasing by Molecular Replacement 93%
- Fragment-based screening targeting an open form of the SARS-CoV-2 main protease binding pocket 93%
Similar papers in this journal
- The Crystal Structure of Bromide-bound GtACR1 Reveals a Pre-Activated State in the Transmembrane Anion Tunnel 94%
- Water and chloride as allosteric inhibitors in WNK kinase osmosensing 93%
- X-Ray Structure and enzymatic study of a Bacterial NADPHoxidase highlight the activation mechanism of eukaryoticNOX 93%
Similar papers in this journal
- Integrative Vectors for Regulated Expression of SARS-CoV-2 Proteins Implicated in RNA Metabolism 88%
- The lipid transfer protein Saposin B does not directly bind CD1d for lipid antigen loading 88%
- A commercial antibody to the human condensin II subunit NCAPH2 cross-reacts with a SWI/SNF complex component 87%
"Similar papers" are the closest papers from that journal in the model's embedding space. They show what the match is built on, but the ranking comes mostly from a classifier over the whole training set, not from these examples alone.