3C6D
The pseudo-atomic structure of dengue immature virus
Summary for 3C6D
| Entry DOI | 10.2210/pdb3c6d/pdb |
| Related | 3C5X |
| EMDB information | 5102 |
| Descriptor | Polyprotein, prM (2 entities in total) |
| Functional Keywords | icosahedral virion, helicase, hydrolase, nucleotide-binding, rna replication, transmembrane, atp-binding, capsid protein, cleavage on pair of basic residues, endoplasmic reticulum, envelope protein, glycoprotein, metal-binding, multifunctional enzyme, nucleotidyltransferase, nucleus, phosphoprotein, protease, ribonucleoprotein, rna-binding, rna-directed rna polymerase, secreted, serine protease, transcription, transcription regulation, transferase, viral nucleoprotein, icosahedral virus, virus |
| Biological source | Dengue virus 2 Thailand/16681/84 More |
| Total number of polymer chains | 6 |
| Total formula weight | 159497.82 |
| Authors | |
| Primary citation | Li, L.,Lok, S.M.,Yu, I.M.,Zhang, Y.,Kuhn, R.J.,Chen, J.,Rossmann, M.G. The flavivirus precursor membrane-envelope protein complex: structure and maturation Science, 319:1830-1834, 2008 Cited by PubMed Abstract: Many viruses go through a maturation step in the final stages of assembly before being transmitted to another host. The maturation process of flaviviruses is directed by the proteolytic cleavage of the precursor membrane protein (prM), turning inert virus into infectious particles. We have determined the 2.2 angstrom resolution crystal structure of a recombinant protein in which the dengue virus prM is linked to the envelope glycoprotein E. The structure represents the prM-E heterodimer and fits well into the cryo-electron microscopy density of immature virus at neutral pH. The pr peptide beta-barrel structure covers the fusion loop in E, preventing fusion with host cell membranes. The structure provides a basis for identifying the stages of its pH-directed conformational metamorphosis during maturation, ending with release of pr when budding from the host. PubMed: 18369147DOI: 10.1126/science.1153263 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (12.5 Å) |
Structure validation
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