Abstract
Sialic acid (Sia) at the cell surface is a putative SARS-CoV-2 co-receptor via interactions with Spike N-terminal domain (NTD), and Sia-based inhibitors have shown efficacy against SARS-CoV-2 in culture. However, protein:small-molecule complexes pose difficult cryo-EM targets because small ligands typically act in relatively poorly resolved peripheral regions, and structural details of Spike:Sia interactions via the highly flexible NTD remain elusive. Spike receptor-binding domain (RBD) binds linoleic acid (LA), which interacts with neighboring RBD to lock-in a closed trimer with rigid, well-resolved NTDs. While endogenous LA from certain expression systems serendipitously permits visualization of bound Sia, necessary and sufficient conditions for reliable extraction of this complex remain unclear.
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callSimilar Papers
More From: Biophysical Journal
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
