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2jsf

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==Solution structures of the envelope protein domain III from the dengue-2 virus==
==Solution structures of the envelope protein domain III from the dengue-2 virus==
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<StructureSection load='2jsf' size='340' side='right' caption='[[2jsf]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
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<StructureSection load='2jsf' size='340' side='right'caption='[[2jsf]]' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[2jsf]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Dengue_virus_2 Dengue virus 2]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JSF OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2JSF FirstGlance]. <br>
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<table><tr><td colspan='2'>[[2jsf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Dengue_virus_2 Dengue virus 2]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2JSF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2JSF FirstGlance]. <br>
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</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=2jsf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jsf OCA], [http://pdbe.org/2jsf PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2jsf RCSB], [http://www.ebi.ac.uk/pdbsum/2jsf PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2jsf ProSAT]</span></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 20 models</td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2jsf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2jsf OCA], [https://pdbe.org/2jsf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2jsf RCSB], [https://www.ebi.ac.uk/pdbsum/2jsf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2jsf ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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[[http://www.uniprot.org/uniprot/POLG_DEN2U POLG_DEN2U]] 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. 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).
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[https://www.uniprot.org/uniprot/POLG_DEN2U POLG_DEN2U] 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. 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).
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Dengue virus 2]]
[[Category: Dengue virus 2]]
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[[Category: Cheng, J]]
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[[Category: Large Structures]]
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[[Category: Huang, K]]
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[[Category: Cheng J]]
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[[Category: Domain iii]]
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[[Category: Huang K]]
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[[Category: Viral protein]]
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Current revision

Solution structures of the envelope protein domain III from the dengue-2 virus

PDB ID 2jsf

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