4r8t: Difference between revisions

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'''Unreleased structure'''
==Structure of JEV protease==
 
<StructureSection load='4r8t' size='340' side='right' caption='[[4r8t]], [[Resolution|resolution]] 2.13&Aring;' scene=''>
The entry 4r8t is ON HOLD
== Structural highlights ==
 
<table><tr><td colspan='2'>[[4r8t]] is a 2 chain structure. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4R8T FirstGlance]. <br>
Authors: Nair, D.T., Weinert, T., Wang, M., Oligeric, V.
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene></td></tr>
 
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4r8t FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4r8t OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4r8t RCSB], [http://www.ebi.ac.uk/pdbsum/4r8t PDBsum]</span></td></tr>
Description: Structure of JEV protease
</table>
== Function ==
[[http://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).
__TOC__
</StructureSection>
[[Category: Nair, D T]]
[[Category: Oligeric, V]]
[[Category: Wang, M]]
[[Category: Weinert, T]]
[[Category: Hydrolase]]
[[Category: Ns2b]]
[[Category: Protease]]
[[Category: Serine protease]]