7LTU
AALALL SEGMENT FROM THE NUCLEOPROTEIN OF SARS-COV-2, RESIDUES 217-222, CRYSTAL FORM 1
Summary for 7LTU
Entry DOI | 10.2210/pdb7ltu/pdb |
Descriptor | AALALL SEGMENT FROM THE NUCLEOPROTEIN OF SARS-COV-2,RESIDUES 217-222, trifluoroacetic acid (3 entities in total) |
Functional Keywords | amyloid fibril, protein fibril |
Biological source | SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS 2 (2019-NCOV, SARS-COV-2) |
Total number of polymer chains | 2 |
Total formula weight | 1483.51 |
Authors | Zee, C.-T.,Sawaya, M.R.,Rodriguez, J.A.,Eisenberg, D.S. (deposition date: 2021-02-20, release date: 2021-03-17, Last modification date: 2024-04-03) |
Primary citation | Tayeb-Fligelman, E.,Cheng, X.,Tai, C.,Bowler, J.T.,Griner, S.,Sawaya, M.R.,Seidler, P.M.,Jiang, Y.X.,Lu, J.,Rosenberg, G.M.,Salwinski, L.,Abskharon, R.,Zee, C.T.,Hou, K.,Li, Y.,Boyer, D.R.,Murray, K.A.,Falcon, G.,Anderson, D.H.,Cascio, D.,Saelices, L.,Damoiseaux, R.,Guo, F.,Eisenberg, D.S. Inhibition of amyloid formation of the Nucleoprotein of SARS-CoV-2. Biorxiv, 2021 Cited by PubMed Abstract: The SARS-CoV-2 Nucleoprotein (NCAP) functions in RNA packaging during viral replication and assembly. Computational analysis of its amino acid sequence reveals a central low-complexity domain (LCD) having sequence features akin to LCDs in other proteins known to function in liquid-liquid phase separation. Here we show that in the presence of viral RNA, NCAP, and also its LCD segment alone, form amyloid-like fibrils when undergoing liquid-liquid phase separation. Within the LCD we identified three 6-residue segments that drive amyloid fibril formation. We determined atomic structures for fibrils formed by each of the three identified segments. These structures informed our design of peptide inhibitors of NCAP fibril formation and liquid-liquid phase separation, suggesting a therapeutic route for Covid-19. PubMed: 33688654DOI: 10.1101/2021.03.05.434000 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.122 Å) |
Structure validation
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