3nxg
JC polyomavirus VP1JC polyomavirus VP1
Template:ABSTRACT PUBMED 20951965
FunctionFunction
[VP1_POVJC] Forms an icosahedral capsid with a T=7 symmetry and a 40 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 a N-linked glycoprotein containing terminal alpha(2-6)-linked sialic acids on the cell surface to provide virion attachment to target cell. The serotonergic receptor 5HT2AR also acts as a cellular receptor for JCV on human glial cells. Once attached, the virions enter predominantly by a ligand-inducible clathrin-dependent pathway and traffic to the ER. 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 at nuclear domains called promyelocytic leukemia (PML) bodies, and participates in rearranging nucleosomes around the viral DNA.[1]
About this StructureAbout this Structure
3nxg is a 5 chain structure with sequence from Jc polyomavirus. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ Neu U, Maginnis MS, Palma AS, Stroh LJ, Nelson CD, Feizi T, Atwood WJ, Stehle T. Structure-function analysis of the human JC polyomavirus establishes the LSTc pentasaccharide as a functional receptor motif. Cell Host Microbe. 2010 Oct 21;8(4):309-19. PMID:20951965 doi:10.1016/j.chom.2010.09.004