Author: Courtney Mycroft-West; Dunhao Su; Stefano Elli; Scott Guimond; Gavin Miller; Jeremy Turnbull; Edwin Yates; Marco Guerrini; David Fernig; Marcelo Lima; Mark Skidmore
Title: The 2019 coronavirus (SARS-CoV-2) surface protein (Spike) S1 Receptor Binding Domain undergoes conformational change upon heparin binding Document date: 2020_3_2
ID: 0d77ojnb_24
Snippet: Studying SARS-CoV-2 Spike protein structure and behaviour in solution is a vital step for the development of effective therapeutics against SARS-CoV-2. Here, the ability of the SARS-CoV-2 S1 RBD to bind pharmaceutical heparin has been studied using spectroscopic techniques in concert with molecular modelling. The data show that SARS-CoV-2 S1 RBD binds to heparin and that upon binding, a significant structural change is induced. Moreover, moieties.....
Document: Studying SARS-CoV-2 Spike protein structure and behaviour in solution is a vital step for the development of effective therapeutics against SARS-CoV-2. Here, the ability of the SARS-CoV-2 S1 RBD to bind pharmaceutical heparin has been studied using spectroscopic techniques in concert with molecular modelling. The data show that SARS-CoV-2 S1 RBD binds to heparin and that upon binding, a significant structural change is induced. Moreover, moieties of basic amino acid residues, known to constitute heparin binding domains, are solvent accessible on the SARS-CoV-2 S1 RBD surface and form a continuous patch that is suitable for heparin binding.
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