4r8t

== Structural highlights ==

== Structural highlights ==

<table><tr><td colspan='2'>[[4r8t]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Japanese_encephalitis_virus Japanese encephalitis virus] and [https://en.wikipedia.org/wiki/Japanese_encephalitis_virus_strain_Nakayama Japanese encephalitis virus strain Nakayama]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R8T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4R8T FirstGlance]. <br>

<table><tr><td colspan='2'>[[4r8t]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Japanese_encephalitis_virus Japanese encephalitis virus] and [https://en.wikipedia.org/wiki/Japanese_encephalitis_virus_strain_Nakayama Japanese encephalitis virus strain Nakayama]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4R8T OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4R8T FirstGlance]. <br>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4r8t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r8t OCA], [https://pdbe.org/4r8t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4r8t RCSB], [https://www.ebi.ac.uk/pdbsum/4r8t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4r8t ProSAT]</span></td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4r8t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r8t OCA], [https://pdbe.org/4r8t PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4r8t RCSB], [https://www.ebi.ac.uk/pdbsum/4r8t PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4r8t ProSAT]</span></td></tr>

</table>

</table>

== Function ==

== Function ==

[https://www.uniprot.org/uniprot/POLG_JAEVN POLG_JAEVN] Capsid protein C self-assembles to form an icosahedral capsid about 30 nm in diameter. The capsid encapsulates the genomic RNA (By similarity). 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). 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). Non-structural protein 1 is involved in virus replication and regulation of the innate immune response. Non-structural protein 2A may be involved viral RNA replication and capsid assembly. Non-structural protein 2B is a required cofactor for the serine protease function of NS3.[PROSITE-ProRule:PRU00859] 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).

[https://www.uniprot.org/uniprot/POLG_JAEVN POLG_JAEVN] Capsid protein C self-assembles to form an icosahedral capsid about 30 nm in diameter. The capsid encapsulates the genomic RNA (By similarity). 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). 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). Non-structural protein 1 is involved in virus replication and regulation of the innate immune response. Non-structural protein 2A may be involved viral RNA replication and capsid assembly. Non-structural protein 2B is a required cofactor for the serine protease function of NS3.[PROSITE-ProRule:PRU00859] 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).

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</StructureSection>

</StructureSection>