7IC0
PanDDA analysis group deposition -- SARS-CoV-2 Nsp1 crystal Apo08 (dataset 1) from the KIT library screening campaign, data used for ground state calculation
Summary for 7IC0
| Entry DOI | 10.2210/pdb7ic0/pdb |
| Group deposition | PanDDA analysis group deposition of SARS-CoV-2 Nsp1 soaked with fragments from the KIT library (G_1002337) |
| Descriptor | Host translation inhibitor nsp1 (2 entities in total) |
| Functional Keywords | sars-cov-2, fragment screen, nsp1, kit library, viral protein |
| Biological source | Severe acute respiratory syndrome coronavirus 2 |
| Total number of polymer chains | 1 |
| Total formula weight | 12863.85 |
| Authors | |
| Primary citation | Lennartz, F.,Wollenhaupt, J.,Oelker, M.,Froling, P.,Mueller, U.,Deckers, A.,Grathwol, C.,Brase, S.,Jung, N.,Weiss, M.S. Crystallographic fragment screening against SARS-CoV-2 nonstructural protein 1 using the F2X-Entry Screen and a newly developed fragment library. Acta Crystallogr D Struct Biol, 2025 Cited by PubMed Abstract: Severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) continues to threaten global health. This underpins the need for novel therapeutics against this virus. Nonstructural protein 1 (Nsp1) of SARS-CoV-2 is a multifunctional protein with an essential role in viral replication. As such, it presents itself as an attractive target for drug discovery. Here, we describe two crystallographic fragment-screening campaigns against Nsp1, one using the established F2X-Entry Screen and one using a new, chemically and structurally diverse fragment library, which we call the KIT library. Together, 21 hits could be identified from 192 screened fragments, which constitutes the highest hit rate reported for Nsp1 to date. Many hits bind to a key functional region and interact with residues involved in cellular mRNA cleavage, ribosome binding and viral RNA recognition. Furthermore, most of the identified fragments share a common binding mode, providing promising starting points for further optimization into drug-like compounds that can disrupt the role of Nsp1 in viral replication. PubMed: 41081353DOI: 10.1107/S2059798325008563 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.84 Å) |
Structure validation
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