This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
1bev
From Proteopedia
Revision as of 03:06, 7 August 2014 by OCA (Talk | contribs)
1bev is a 4 chain structure with sequence from Viruses. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Smyth M, Tate J, Hoey E, Lyons C, Martin S, Stuart D. Implications for viral uncoating from the structure of bovine enterovirus. Nat Struct Biol. 1995 Mar;2(3):224-31. PMID:7773791
