8DQU
Nanobody bound SARS-CoV-2 Nsp9
Summary for 8DQU
| Entry DOI | 10.2210/pdb8dqu/pdb |
| Descriptor | Nanobody, Non-structural protein 9 (3 entities in total) |
| Functional Keywords | sars-cov-2, nsp9, nanobody, viral protein |
| Biological source | Lama glama More |
| Total number of polymer chains | 4 |
| Total formula weight | 56691.53 |
| Authors | Littler, D.R.,Gully, B.S.,Rossjohn, J. (deposition date: 2022-07-20, release date: 2023-02-08, Last modification date: 2024-11-06) |
| Primary citation | Pan, Y.,Chandrashekaran, I.R.,Tennant, L.,Rossjohn, J.,Littler, D.R. Inside-out: Antibody-binding reveals potential folding hinge-points within the SARS-CoV-2 replication co-factor nsp9. Plos One, 18:e0283194-e0283194, 2023 Cited by PubMed Abstract: Nsp9 is a conserved accessory component of the coronaviral replication and transcription complex. It is the predominant substrate of nsp12's nucleotidylation activity while also serving to recruit proteins required for viral 5'-capping. Anti-nsp9 specific nanobodies have been isolated previously. We confirm that their binding mode is centred upon Trp-53 within SARS-CoV-2 nsp9. Antibody binding at this site surprisingly results in large-scale changes to the overall topology of this coronaviral unique fold. We further characterise the antibody-induced structural dynamism within nsp9, identifying a number of potentially flexible regions. A large expansion of the cavity between the s2-s3 and s4-s5 loops is particularly noteworthy. As is the potential for large-scale movements in the C-terminal GxxxG helix. PubMed: 37036856DOI: 10.1371/journal.pone.0283194 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.45003185971 Å) |
Structure validation
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