1SSK
Structure of the N-terminal RNA-binding Domain of the SARS CoV Nucleocapsid Protein
Summary for 1SSK
| Entry DOI | 10.2210/pdb1ssk/pdb |
| Descriptor | Nucleocapsid protein (1 entity in total) |
| Functional Keywords | nucleocapsid protein, structural protein |
| Biological source | SARS coronavirus |
| Cellular location | Virion: P59595 |
| Total number of polymer chains | 1 |
| Total formula weight | 17179.03 |
| Authors | Huang, Q.,Yu, L.,Petros, A.M.,Gunasekera, A.,Liu, Z.,Xu, N.,Hajduk, P.,Mack, J.,Fesik, S.W.,Olejniczak, E.T. (deposition date: 2004-03-24, release date: 2004-06-08, Last modification date: 2024-05-22) |
| Primary citation | Huang, Q.,Yu, L.,Petros, A.M.,Gunasekera, A.,Liu, Z.,Xu, N.,Hajduk, P.,Mack, J.,Fesik, S.W.,Olejniczak, E.T. Structure of the N-Terminal RNA-Binding Domain of the SARS CoV Nucleocapsid Protein. Biochemistry, 43:6059-6063, 2004 Cited by PubMed Abstract: The severe acute respiratory syndrome (SARS) virus belongs to the Coronaviridea family of viruses. Its virion encodes several proteins including a replicase and four structural proteins. Here we describe the three-dimensional structure of the N-terminal domain of the SARS coronavirus (CoV) nucleocapsid protein. The protein consists of a five-stranded beta sheet with a folding topology distinct from other RNA-binding proteins. Single-stranded RNAs bind to the protein surface at the junction between a flexible, positively charged beta hairpin and the core structure. NMR-based screening was used to identify low molecular weight compounds that bind to this site. PubMed: 15147189DOI: 10.1021/bi036155b PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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