1bev: Difference between revisions

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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"

<applet load="1bev" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

caption="1bev, resolution 3.0Å" />

'''BOVINE ENTEROVIRUS VG-5-27'''<br />

==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.

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 [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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1BEV OCA].

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==

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[[Category: picornavirus]]

''Page seeded by [http://~~ispc~~.weizmann.ac.il/oca OCA ] on ~~Sun Nov 18 09~~:26:~~27 2007~~''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:54:31 2008''

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@@ Line 1: / Line 1: @@
-[[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"
-<applet load="1bev" size="450" color="white" frame="true" align="right" spinBox="true"
 caption="1bev, resolution 3.0&Aring;" />
 '''BOVINE ENTEROVIRUS VG-5-27'''<br />
 ==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.
+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==
-BEV 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BEV OCA].
+BEV 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==
@@ Line 27: / Line 26: @@
 [[Category: picornavirus]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 18 09:26:27 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:54:31 2008''