3iys

Homology model of avian polyomavirus asymmetric unit

Loading... Status: waiting for Mol* initialization Structural highlights 3iys is a 6 chain structure with sequence from Aves polyomavirus 1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 11.3Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function VP1_BFPYV Forms an icosahedral capsid with a T=7 symmetry and a 46-48 nm diameter. The capsid is composed of 72 pentamers linked to each other by disulfide bonds and associated with VP2 or VP3 proteins. Interacts with sialic acids on the cell surface to provide virion attachment to target cell. Once attached, the virion is internalized by endocytosis and traffics to the endoplasmic reticulum. Inside the endoplasmic reticulum, the protein folding machinery isomerizes VP1 interpentamer disulfide bonds, thereby triggering initial uncoating. Next, the virion uses the endoplasmic reticulum-associated degradation machinery to probably translocate in the cytosol before reaching the nucleus. Nuclear entry of the viral DNA involves the selective exposure and importin recognition of VP2/Vp3 nuclear localization signal. In late phase of infection, neo-synthesized VP1 encapsulates replicated genomic DNA in the nucleus, and participates in rearranging nucleosomes around the viral DNA (By similarity). See Also Virus coat proteins 3D structures

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