1bev
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(New page: 200px<br /> <applet load="1bev" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bev, resolution 3.0Å" /> '''BOVINE ENTEROVIRUS V...)
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Revision as of 07:19, 18 November 2007
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BOVINE ENTEROVIRUS VG-5-27
Overview
We have determined the crystal structure of a bovine enterovirus, revealing that the topologies of the major capsid proteins and the overall, architecture of the virion are similar to those of related picornaviruses., The external loops joining beta-strands are truncated and the canyon, region is partially filled by an extension of the VP3 G-H loop giving the, viral capsid a relatively smooth appearance. These changes may have, implications for cell attachment. In spite of these differences the virus, maintains a hydrophobic pocket within VP1, occupied by a specific 'pocket, factor' which appears to be myristic acid. These observations support the, proposal that a kinetic equilibrium exists between occupied and unoccupied, pocket states, with occupation inhibiting uncoating.
About this Structure
1BEV is a Protein complex structure of sequences from Bovine enterovirus with SO4 and MYR as ligands. Full crystallographic information is available from OCA.
Reference
Implications for viral uncoating from the structure of bovine enterovirus., Smyth M, Tate J, Hoey E, Lyons C, Martin S, Stuart D, Nat Struct Biol. 1995 Mar;2(3):224-31. PMID:7773791
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