| Home > Publications database > Nucleotide-bound crystal structures of the SARS-CoV-2 helicase NSP13 |
| Journal Article | PUBDB-2025-04027 |
; ; ;
2025
Blackwell
Oxford [u.a.]
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Please use a persistent id in citations: doi:10.1107/S2053230X25005266 doi:10.3204/PUBDB-2025-04027
Abstract: Nucleotide-bound crystal structures of SARS-CoV-2 NSP13 in ADP- and ATP-bound states were resolved to 1.8 and 1.9 Å, respectively. The ADP-bound model captures a state immediately following ATP hydrolysis, with both ADP and orthophosphate still present in the active site. Further comparative analysis revealed that crystal packing influences NSP13 by stabilizing the nucleotide-binding site, underscoring the importance of accounting for these effects in structure-based drug design targeting NSP13.
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