1tme
From Proteopedia
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THREE-DIMENSIONAL STRUCTURE OF THEILER VIRUS
Overview
Theiler murine encephalomyelitis virus strains are categorized into two, groups, a neurovirulent group that rapidly kills the host, and a, demyelinating group that causes a generally nonlethal infection of motor, neurons followed by a persistent infection of the white matter with, demyelinating lesions similar to those found in multiple sclerosis. The, three-dimensional structure of the DA strain, a member of the, demyelinating group, has been determined at 2.8 A resolution. As in other, picornaviruses, the icosahedral capsid is formed by the packing of, wedge-shaped eight-stranded antiparallel beta barrels. The surface of, Theiler virus has large star-shaped plateaus at the fivefold axes and, broad depressions spanning the twofold axes. Several unusual structural, features are clustered near one edge of the depression. These include two, finger-like loops projecting from the surface (one formed by residues, 78-85 of VP1, and the other formed by residues 56-65 of VP3) and a third, loop containing three cysteines (residues 87, 89, and 91 of VP3), which, appear to be covalently modified. Most of the sequence differences between, the demyelinating and neurovirulent groups that could play a role in, determining pathogenesis map to the surface of the star-shaped plateau., The distribution of these sequence differences on the surface of the, virion is consistent with models in which the differences in the, pathogenesis of the two groups of Theiler viruses are the result of, differences in immunological or receptor-mediated recognition processes.
About this Structure
1TME is a Protein complex structure of sequences from Theiler's murine encephalomyelitis virus. Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of Theiler virus., Grant RA, Filman DJ, Fujinami RS, Icenogle JP, Hogle JM, Proc Natl Acad Sci U S A. 1992 Mar 15;89(6):2061-5. PMID:1549565
Page seeded by OCA on Wed Nov 21 03:24:27 2007
