1B35
CRICKET PARALYSIS VIRUS (CRPV)
Summary for 1B35
Entry DOI | 10.2210/pdb1b35/pdb |
Descriptor | PROTEIN (CRICKET PARALYSIS VIRUS, VP1), PROTEIN (CRICKET PARALYSIS VIRUS, VP2), PROTEIN (CRICKET PARALYSIS VIRUS, VP3), ... (5 entities in total) |
Functional Keywords | insect picorna-like virus, icosahedral virus, virus |
Biological source | Cricket paralysis virus More |
Cellular location | Capsid protein 1: Virion. Capsid protein 4: Virion. Capsid protein 2: Virion. Capsid protein 3: Virion: P13418 P13418 P13418 P13418 |
Total number of polymer chains | 4 |
Total formula weight | 95412.50 |
Authors | Tate, J.G.,Liljas, L.,Scotti, P.D.,Christian, P.D.,Lin, T.W.,Johnson, J.E. (deposition date: 1998-12-17, release date: 1999-08-09, Last modification date: 2023-08-09) |
Primary citation | Tate, J.,Liljas, L.,Scotti, P.,Christian, P.,Lin, T.,Johnson, J.E. The crystal structure of cricket paralysis virus: the first view of a new virus family. Nat.Struct.Biol., 6:765-774, 1999 Cited by PubMed Abstract: Numerous small, RNA-containing insect viruses are currently classified as picornaviruses, or as 'picorna-like', since they superficially resemble the true picornaviruses. Considerable evidence now suggests that several of these viruses are members of a distinct family. We have determined the gene sequence of the capsid proteins and the 2.4 A resolution crystal structure of the cricket paralysis virus. While the genome sequence indicates that the insect picorna-like viruses represent a distinct lineage compared to true picornaviruses, the capsid structure demonstrates that the two groups are related. These viral genomes are, thus, best viewed as composed of exchangeable modules that have recombined. PubMed: 10426956DOI: 10.1038/11543 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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