3c5x

Crystal structure of the precursor membrane protein- envelope protein heterodimer from the dengue 2 virus at low pH

spinqualitylabelsall models 3c5x, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3c5x is a 2 chain structure with sequence from Dengue virus 2 and Dengue virus 2 Thailand/16681/84. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.2Å Ligands: BMA, NAG, NDG, SHD Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q6H1E5_9FLAV Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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