TY  - INPR
A1  - Ni, Xiaomin
A1  - Schröder, Martin
A1  - Olieric, Vincent
A1  - Sharpe, May E.
A1  - Olmos, Hernandez-Olmos
A1  - Proschak, Ewgenij
A1  - Merk, Daniel
A1  - Knapp, Stefan
A1  - Chaikuad, Apirat
T1  - Structural insights into plasticity and discovery of remdesivir metabolite GS-441524 binding in SARS-CoV-2 macrodomain
T2  - bioRxiv
N2  - The nsP3 macrodomain is a conserved protein interaction module that plays essential regulatory roles in host immune response by recognizing and removing posttranslational ADP-ribosylation sites during SARS-CoV-2 infection. Thus, targeting this protein domain may offer a therapeutic strategy to combat the current and future virus pandemics. To assist inhibitor development efforts, we report here a comprehensive set of macrodomain crystal structures complexed with diverse naturally-occurring nucleotides, small molecules as well as nucleotide analogues including GS-441524 and its phosphorylated analogue, active metabolites of remdesivir. The presented data strengthen our understanding of the SARS-CoV-2 macrodomain structural plasticity and it provides chemical starting points for future inhibitor development.
Y1  - 2021
UR  - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/72867
UR  - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-728674
IS  - 2021.03.04.433966
ER  -