6wy1

<table><tr><td colspan='2'>[[6wy1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Dengue_virus_2 Dengue virus 2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6WY1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6WY1 FirstGlance]. <br>

== Function ==

[https://www.uniprot.org/uniprot/POLG_DEN26 POLG_DEN26] prM acts as a chaperone for envelope protein E during intracellular virion assembly by masking and inactivating envelope protein E fusion peptide. prM is matured in the last step of virion assembly, presumably to avoid catastrophic activation of the viral fusion peptide induced by the acidic pH of the trans-Golgi network. After cleavage by host furin, the pr peptide is released in the extracellular medium and small envelope protein M and envelope protein E homodimers are dissociated (By similarity).<ref>PMID:15956546</ref> <ref>PMID:16544248</ref> <ref>PMID:15944325</ref> <ref>PMID:19850911</ref> <ref>PMID:19754307</ref> <ref>PMID:19272179</ref> Envelope protein E binding to host cell surface receptor is followed by virus internalization through clathrin-mediated endocytosis. Envelope protein E is subsequently involved in membrane fusion between virion and host late endosomes. Synthesized as a homodimer with prM which acts as a chaperone for envelope protein E. After cleavage of prM, envelope protein E dissociate from small envelope protein M and homodimerizes (By similarity).<ref>PMID:15956546</ref> <ref>PMID:16544248</ref> <ref>PMID:15944325</ref> <ref>PMID:19850911</ref> <ref>PMID:19754307</ref> <ref>PMID:19272179</ref> Non-structural protein 1 is involved in virus replication and regulation of the innate immune response. Soluble and membrane-associated NS1 may activate human complement and induce host vascular leakage. This effect might explain the clinical manifestations of dengue hemorrhagic fever and dengue shock syndrome (By similarity).<ref>PMID:15956546</ref> <ref>PMID:16544248</ref> <ref>PMID:15944325</ref> <ref>PMID:19850911</ref> <ref>PMID:19754307</ref> <ref>PMID:19272179</ref> Non-structural protein 2A may be involved viral RNA replication and capsid assembly (Potential).<ref>PMID:15956546</ref> <ref>PMID:16544248</ref> <ref>PMID:15944325</ref> <ref>PMID:19850911</ref> <ref>PMID:19754307</ref> <ref>PMID:19272179</ref> Non-structural protein 2B is a required cofactor for the serine protease function of NS3 (By similarity).<ref>PMID:15956546</ref> <ref>PMID:16544248</ref> <ref>PMID:15944325</ref> <ref>PMID:19850911</ref> <ref>PMID:19754307</ref> <ref>PMID:19272179</ref> Serine protease NS3 displays three enzymatic activities: serine protease, NTPase and RNA helicase. NS3 serine protease, in association with NS2B, performs its autocleavage and cleaves the polyprotein at dibasic sites in the cytoplasm: C-prM, NS2A-NS2B, NS2B-NS3, NS3-NS4A, NS4A-2K and NS4B-NS5. NS3 RNA helicase binds RNA and unwinds dsRNA in the 3' to 5' direction (By similarity).<ref>PMID:15956546</ref> <ref>PMID:16544248</ref> <ref>PMID:15944325</ref> <ref>PMID:19850911</ref> <ref>PMID:19754307</ref> <ref>PMID:19272179</ref> Non-structural protein 4A induces host endoplasmic reticulum membrane rearrangements leading to the formation of virus-induced membranous vesicles hosting the dsRNA and polymerase, functioning as a replication complex. NS4A might also regulate the ATPase activity of the NS3 helicase (By similarity).<ref>PMID:15956546</ref> <ref>PMID:16544248</ref> <ref>PMID:15944325</ref> <ref>PMID:19850911</ref> <ref>PMID:19754307</ref> <ref>PMID:19272179</ref> Peptide 2k functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter (By similarity).<ref>PMID:15956546</ref> <ref>PMID:16544248</ref> <ref>PMID:15944325</ref> <ref>PMID:19850911</ref> <ref>PMID:19754307</ref> <ref>PMID:19272179</ref> Non-structural protein 4B inhibits interferon (IFN)-induced host STAT1 phosphorylation and nuclear translocation, thereby preventing the establishment of cellular antiviral state by blocking the IFN-alpha/beta pathway.<ref>PMID:15956546</ref> <ref>PMID:16544248</ref> <ref>PMID:15944325</ref> <ref>PMID:19850911</ref> <ref>PMID:19754307</ref> <ref>PMID:19272179</ref> RNA-directed RNA polymerase NS5 replicates the viral (+) and (-) genome, and performs the capping of genomes in the cytoplasm. NS5 methylates viral RNA cap at guanine N-7 and ribose 2'-O positions. Besides its role in genome replication, also prevents the establishment of cellular antiviral state by blocking the interferon-alpha/beta (IFN-alpha/beta) signaling pathway. Inhibits host TYK2 and STAT2 phosphorylation, thereby preventing activation of JAK-STAT signaling pathway (By similarity).<ref>PMID:15956546</ref> <ref>PMID:16544248</ref> <ref>PMID:15944325</ref> <ref>PMID:19850911</ref> <ref>PMID:19754307</ref> <ref>PMID:19272179</ref> Capsid protein C self-assembles to form an icosahedral capsid about 30 nm in diameter. The capsid encapsulates the genomic RNA (By similarity).<ref>PMID:15956546</ref> <ref>PMID:16544248</ref> <ref>PMID:15944325</ref> <ref>PMID:19850911</ref> <ref>PMID:19754307</ref> <ref>PMID:19272179</ref>

[[Category: Dengue virus 2]]