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https://bar.utoronto.ca/thalemine/service/ is incorrect| Description | This entry represents viral capsid proteins from group I dsDNA viruses, including Papovaviridae-like Polyomaviruses and Papillomaviruses. Virus-encoded capsid proteins play a major role in the life cycles of all viruses. Structures have been determined for the major capsid protein VP1 (viral protein 1) from Murine polyomavirus (strain P16 small-plaque) (MPyV) [ ] and the major late protein L1 from Human papillomavirus (HPV) []. These capsid proteins share a β-sandwich topology. Characteristic interactions between the domains of this fold allows the formation of 5-fold and pseudo 6-fold assemblies.Polyomaviruses are dsDNA viruses with no RNA stage in their life cycle. The virus capsid is composed of 72 icosahedral units, each of which is composed of five copies of VP1. The virus attaches to the cell surface by recognition of oligosaccharides terminating in alpha(2,3)-linked sialic acid. The capsid protein VP1 forms a pentamer. The complete capsid is composed of 72 VP1 pentamers, with a minor capsid protein, VP2 or VP3, inserted into the centre of each pentamer like a hairpin. This structure restricts the exposure of internal proteins during viral entry. Polyomavirus coat assembly is rigorously controlled by chaperone-mediated assembly. During viral infection, the heat shock chaperone hsc70 binds VP1 and co-localises it in the nucleus, thereby regulating capsid assembly [ ].Papillomaviruses are members of the papovavirus superfamily. More than 70 different types of papillomavirus have been discovered in humans, some of which have been shown to cause genital carcinomas and cutaneous warts [ ]. The viruses contain a circular dsDNA genome surrounded by an icosahedral capsid (non-enveloped). Two proteins are involved in capsid formation: a major (L1) and a minor (L2) protein, in the approximate proportion 95:5%. L1 forms a pentameric assembly unit of the viral shell in a manner that closely resembles VP1 from polyomaviruses. Intermolecular disulphide bonding holds the L1 capsid proteins together []. L1 capsid proteins can bind via its nuclear localisation signal (NLS) to karyopherins Kapbeta(2) and Kapbeta(3) and inhibit the Kapbeta(2) and Kapbeta(3) nuclear import pathways during the productive phase of the viral life cycle []. Surface loops on L1 pentamers contain sites of sequence variation between HPV types. | Name | Double-stranded DNA virus, group I, capsid |
| Short Name | dsDNA_vir_gr_I_capsid | Type | Homologous_superfamily |
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