4O6H
2.8A crystal structure of Lymphocytic Choriomeningitis Virus Nucleoprotein C-terminal Domain
Summary for 4O6H
Entry DOI | 10.2210/pdb4o6h/pdb |
Related | 4O6I |
Descriptor | Nucleoprotein, ZINC ION, IMIDAZOLE, ... (5 entities in total) |
Functional Keywords | exoribonuclease, hydrolase |
Biological source | Lymphocytic choriomeningitis virus (LCMV) |
Cellular location | Virion: P09992 |
Total number of polymer chains | 8 |
Total formula weight | 212254.38 |
Authors | West, B.R.,Hastie, K.M.,Saphire, E.O. (deposition date: 2013-12-20, release date: 2014-06-11, Last modification date: 2023-09-20) |
Primary citation | West, B.R.,Hastie, K.M.,Saphire, E.O. Structure of the LCMV nucleoprotein provides a template for understanding arenavirus replication and immunosuppression. Acta Crystallogr.,Sect.D, 70:1764-1769, 2014 Cited by PubMed Abstract: The X-ray crystal structure of the Lymphocytic choriomeningitis virus nucleoprotein C-terminal immunosuppressive domain (LCMV NPΔ340) was determined to 2.0 Å resolution. The structure indicates that LCMV NPΔ340, like the other structurally characterized arenaviral nucleoproteins, adopts the fold of an exonuclease. This structure provides a crucial three-dimensional template for functional exploration of the replication and immunosuppression of this prototypic arenavirus. PubMed: 24914986DOI: 10.1107/S1399004714007883 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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