1N6G

The structure of immature Dengue-2 prM particles

Summary for 1N6G

• Entry DOI: 10.2210/pdb1n6g/pdb
• Descriptor: major envelope protein E (1 entity in total)
• Functional Keywords: flavivirus, flaviviridae, dengue immature virus, prm particle, icosahedral virus, virus
• Biological source: Dengue virus 2 Puerto Rico/PR159-S1/1969
• Total number of polymer chains: 3
• Total formula weight: 129693.43

Authors

Zhang, Y.,Corver, J.,Chipman, P.R.,Zhang, W.,Pletnev, S.V.,Sedlak, D.,Baker, T.S.,Strauss, J.H.,Kuhn, R.J.,Rossmann, M.G. (deposition date: 2002-11-10, release date: 2003-06-03, Last modification date: 2024-02-14)

Primary citation

Zhang, Y.,Corver, J.,Chipman, P.R.,Zhang, W.,Pletnev, S.V.,Sedlak, D.,Baker, T.S.,Strauss, J.H.,Kuhn, R.J.,Rossmann, M.G.
Structures of Immature flavivirus particles
EMBO J., 22:2604-2613, 2003

PubMed Abstract: Structures of prM-containing dengue and yellow fever virus particles were determined to 16 and 25 A resolution, respectively, by cryoelectron microscopy and image reconstruction techniques. The closely similar structures show 60 icosahedrally organized trimeric spikes on the particle surface. Each spike consists of three prM:E heterodimers, where E is an envelope glycoprotein and prM is the precursor to the membrane protein M. The pre-peptide components of the prM proteins in each spike cover the fusion peptides at the distal ends of the E glycoproteins in a manner similar to the organization of the glycoproteins in the alphavirus spikes. Each heterodimer is associated with an E and a prM transmembrane density. These transmembrane densities represent either an EE or prMprM antiparallel coiled coil by which each protein spans the membrane twice, leaving the C-terminus of each protein on the exterior of the viral membrane, consistent with the predicted membrane-spanning domains of the unprocessed polyprotein.

PubMed: 12773377
DOI: 10.1093/emboj/cdg270

Experimental method

ELECTRON MICROSCOPY (16 Å)