1bev

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{{STRUCTURE_1bev| PDB=1bev | SCENE= }}
{{STRUCTURE_1bev| PDB=1bev | SCENE= }}
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'''BOVINE ENTEROVIRUS VG-5-27'''
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===BOVINE ENTEROVIRUS VG-5-27===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 7773791 is the PubMed ID number.
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{{ABSTRACT_PUBMED_7773791}}
==About this Structure==
==About this Structure==
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[[Category: Icosahedral virus]]
[[Category: Icosahedral virus]]
[[Category: Picornavirus]]
[[Category: Picornavirus]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:00:01 2008''

Revision as of 16:00, 30 June 2008

Image:1bev.png

Template:STRUCTURE 1bev

BOVINE ENTEROVIRUS VG-5-27

Template:ABSTRACT PUBMED 7773791

About this Structure

1BEV is a Protein complex structure of sequences from Bovine enterovirus. 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

Page seeded by OCA on Mon Jun 30 19:00:01 2008

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