1b35
From Proteopedia
Contents |
CRICKET PARALYSIS VIRUS (CRPV)
Template:ABSTRACT PUBMED 10426956
Function
[POLS_CRPVC] Structural polyprotein: precursor of all the viral capsid proteins. Capsid protein 1, together with capsid proteins 2 and 3, form an icosahedral capsid protecting the viral RNA genome. The icosahedral capsid has a pseudo-T=3 symmetry with a diameter of approximately 300 Angstroms, and is composed of 60 copies of each CP1, CP2, and CP3. CP1 is situated at the 12 fivefold axes, whereas CP2 and CP3 are located at the quasi-sixfold axes. All these proteins contain a beta-sheet structure called beta-barrel jelly roll. Capsid protein 4 is a tstructural component of the icosahedral capsid protecting the genomic RNA. It may play an important role in capsid assembly. Capsid protein 2, together with capsid proteins 1 and 3, form an icosahedral capsid protecting the viral RNA genome. The icosahedral capsid has a pseudo-T=3 symmetry with a diameter of approximately 300 Angstroms, and is composed of 60 copies of each CP1, CP2, and CP3. CP1 is situated at the 12 fivefold axes, whereas CP2 and CP3 are located at the quasi-sixfold axes. All these proteins contain a beta-sheet structure called beta-barrel jelly roll. Capsid protein 3, together with capsid proteins 1 and 2, form an icosahedral capsid protecting the viral RNA genome. The icosahedral capsid has a pseudo-T=3 symmetry with a diameter of approximately 300 Angstroms, and is composed of 60 copies of each CP1, CP2, and CP3. CP1 is situated at the 12 fivefold axes, whereas CP2 and CP3 are located at the quasi-sixfold axes. All these proteins contain a beta-sheet structure called beta-barrel jelly roll.
About this Structure
1b35 is a 4 chain structure with sequence from Crpv. Full crystallographic information is available from OCA.
Reference
- Tate J, Liljas L, Scotti P, Christian P, Lin T, Johnson JE. The crystal structure of cricket paralysis virus: the first view of a new virus family. Nat Struct Biol. 1999 Aug;6(8):765-74. PMID:10426956 doi:http://dx.doi.org/10.1038/11543