1n6g
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(New page: 200px<br /><applet load="1n6g" size="450" color="white" frame="true" align="right" spinBox="true" caption="1n6g" /> '''The structure of immature Dengue-2 prM parti...)
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Revision as of 19:53, 20 November 2007
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The structure of immature Dengue-2 prM particles
Overview
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.
About this Structure
1N6G is a Single protein structure of sequence from Dengue virus type 3. Full crystallographic information is available from OCA.
Reference
Structures of immature flavivirus particles., Zhang Y, Corver J, Chipman PR, Zhang W, Pletnev SV, Sedlak D, Baker TS, Strauss JH, Kuhn RJ, Rossmann MG, EMBO J. 2003 Jun 2;22(11):2604-13. PMID:12773377
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