%0 Journal Article
%A Kloskowski, Patrick
%A Neumann, Piotr
%A Kumar, Priya
%A Berndt, Annette
%A Dobbelstein, Matthias
%A Ficner, Ralf
%T Myricetin-bound crystal structure of the SARS-CoV-2 helicase NSP13 facilitates the discovery of novel natural inhibitors
%J Acta crystallographica / Section D
%V 81
%N 6
%@ 0907-4449
%C Bognor Regis
%I Wiley
%M PUBDB-2025-02293
%P 310 - 326
%D 2025
%X The SARS-CoV-2 helicase NSP13 is a highly conserved and essential component of the viral replication machinery, making it a promising target for antiviral drug development. Here, we present the 2 Å resolution crystal structure of NSP13 bound to the natural flavonoid myricetin, revealing a conserved allosteric binding site. Guided by these structural findings, a virtual screening campaign identified the caffeic acid derivatives rosmarinic acid and chlorogenic acid as potential novel natural inhibitors, which were experimentally validated to inhibit RNA-unwinding activity. This study provides structural insights that could support ongoing drug-discovery efforts targeting NSP13 in SARS-CoV-2 and other coronaviruses with pandemic potential.
%F PUB:(DE-HGF)16
%9 Journal Article
%$ pmid:40421686
%R 10.1107/S2059798325004498
%U https://bib-pubdb1.desy.de/record/632965