1bev
From Proteopedia
(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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| - | [[Image:1bev.gif|left|200px]]<br /> | + | [[Image:1bev.gif|left|200px]]<br /><applet load="1bev" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="1bev, resolution 3.0Å" /> | caption="1bev, resolution 3.0Å" /> | ||
'''BOVINE ENTEROVIRUS VG-5-27'''<br /> | '''BOVINE ENTEROVIRUS VG-5-27'''<br /> | ||
==Overview== | ==Overview== | ||
| - | We have determined the crystal structure of a bovine enterovirus, revealing that the topologies of the major capsid proteins and the overall | + | 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== | ==About this Structure== | ||
| - | 1BEV is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bovine_enterovirus Bovine enterovirus] with SO4 and MYR as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1BEV is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Bovine_enterovirus Bovine enterovirus] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=MYR:'>MYR</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BEV OCA]. |
==Reference== | ==Reference== | ||
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[[Category: picornavirus]] | [[Category: picornavirus]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:54:31 2008'' |
Revision as of 09:54, 21 February 2008
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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 and 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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