3c6d
From Proteopedia
The pseudo-atomic structure of dengue immature virus
Overview
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.
About this Structure
3C6D is a Protein complex structure of sequences from Dengue virus 2. Full crystallographic information is available from OCA.
Reference
The flavivirus precursor membrane-envelope protein complex: structure and maturation., Li L, Lok SM, Yu IM, Zhang Y, Kuhn RJ, Chen J, Rossmann MG, Science. 2008 Mar 28;319(5871):1830-4. PMID:18369147
Categories: Dengue virus 2 | Protein complex | Li, L. | Atp-binding | Capsid protein | Cleavage on pair of basic residue | Endoplasmic reticulum | Envelope protein | Glycoprotein | Helicase | Hydrolase | Icosahedral virion | Icosahedral virus | Metal-binding | Multifunctional enzyme | Nucleotide-binding | Nucleotidyltransferase | Nucleus | Phosphoprotein | Protease | Ribonucleoprotein | Rna replication | Rna-binding | Rna-directed rna polymerase | Secreted | Serine protease | Transcription | Transcription regulation | Transferase | Transmembrane | Viral nucleoprotein | Virus
