5IRE
The cryo-EM structure of Zika Virus
Summary for 5IRE
| Entry DOI | 10.2210/pdb5ire/pdb |
| EMDB information | 8116 |
| Descriptor | E protein, M protein, 2-acetamido-2-deoxy-beta-D-glucopyranose-(1-4)-2-acetamido-2-deoxy-beta-D-glucopyranose (3 entities in total) |
| Functional Keywords | zika virus, virus |
| Biological source | Zika virus More |
| Total number of polymer chains | 6 |
| Total formula weight | 190096.01 |
| Authors | Sirohi, D.,Chen, Z.,Sun, L.,Klose, T.,Pierson, T.,Rossmann, M.,Kuhn, R. (deposition date: 2016-03-13, release date: 2016-03-30, Last modification date: 2024-11-13) |
| Primary citation | Sirohi, D.,Chen, Z.,Sun, L.,Klose, T.,Pierson, T.C.,Rossmann, M.G.,Kuhn, R.J. The 3.8 angstrom resolution cryo-EM structure of Zika virus. Science, 352:467-470, 2016 Cited by PubMed Abstract: The recent rapid spread of Zika virus and its unexpected linkage to birth defects and an autoimmune neurological syndrome have generated worldwide concern. Zika virus is a flavivirus like the dengue, yellow fever, and West Nile viruses. We present the 3.8 angstrom resolution structure of mature Zika virus, determined by cryo-electron microscopy (cryo-EM). The structure of Zika virus is similar to other known flavivirus structures, except for the ~10 amino acids that surround the Asn(154) glycosylation site in each of the 180 envelope glycoproteins that make up the icosahedral shell. The carbohydrate moiety associated with this residue, which is recognizable in the cryo-EM electron density, may function as an attachment site of the virus to host cells. This region varies not only among Zika virus strains but also in other flaviviruses, which suggests that differences in this region may influence virus transmission and disease. PubMed: 27033547DOI: 10.1126/science.aaf5316 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.8 Å) |
Structure validation
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