Publication date: Aug 01, 2025
Nucleotide-bound crystal structures of SARS-CoV-2 NSP13 in ADP- and ATP-bound states were resolved to 1. 8 and 1. 9 A, 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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| Concepts | Keywords |
|---|---|
| Atp | ADP-bound structure |
| Crystallogr | ATP-bound structure |
| Genes | COVID-19 |
| Nsp13 | inorganic phosphate |
| Orthophosphate | NSP13 helicase |
| nucleotide-binding sites | |
| SARS-CoV-2 |
Semantics
| Type | Source | Name |
|---|---|---|
| drug | DRUGBANK | ATP |
| drug | DRUGBANK | Phosphate ion |
| disease | IDO | site |
| disease | MESH | COVID 19 |
| disease | IDO | replication |
| disease | IDO | nucleic acid |
| pathway | REACTOME | mRNA Capping |
| pathway | KEGG | Viral replication |
| drug | DRUGBANK | Amino acids |
| disease | IDO | production |
| pathway | REACTOME | Digestion |
| drug | DRUGBANK | Polyethylene glycol |
| drug | DRUGBANK | Magnesium |
| drug | DRUGBANK | Trestolone |
| drug | DRUGBANK | Water |
| drug | DRUGBANK | Ilex paraguariensis leaf |
| disease | IDO | cell |
Original Article
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