3iya

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3iya]] is a 6 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=3IYA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IYA FirstGlance]. <br>
<table><tr><td colspan='2'>[[3iya]] is a 6 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=3IYA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3IYA FirstGlance]. <br>
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</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=3iya FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3iya OCA], [https://pdbe.org/3iya PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3iya RCSB], [https://www.ebi.ac.uk/pdbsum/3iya PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3iya 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">Electron Microscopy, [[Resolution|Resolution]] 22&#8491;</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=3iya FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3iya OCA], [https://pdbe.org/3iya PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3iya RCSB], [https://www.ebi.ac.uk/pdbsum/3iya PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3iya ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
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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).
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[https://www.uniprot.org/uniprot/E7FLK7_9FLAV E7FLK7_9FLAV]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Flavivirus assembles into an inert particle that requires proteolytic activation by furin to enable transmission to other hosts. We previously showed that immature virus undergoes a conformational change at low pH that renders it accessible to furin (I. M. Yu, W. Zhang, H. A. Holdaway, L. Li, V. A. Kostyuchenko, P. R. Chipman, R. J. Kuhn, M. G. Rossmann, and J. Chen, Science 319:1834-1837, 2008). Here we show, using cryoelectron microscopy, that the structure of immature dengue virus at pH 6.0 is essentially the same before and after the cleavage of prM. The structure shows that after cleavage, the proteolytic product pr remains associated with the virion at acidic pH, and that furin cleavage by itself does not induce any major conformational changes. We also show by liposome cofloatation experiments that pr retention prevents membrane insertion, suggesting that pr is present on the virion in the trans-Golgi network to protect the progeny virus from fusion within the host cell.
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Association of the pr peptides with dengue virus at acidic pH blocks membrane fusion.,Yu IM, Holdaway HA, Chipman PR, Kuhn RJ, Rossmann MG, Chen J J Virol. 2009 Dec;83(23):12101-7. Epub 2009 Sep 16. PMID:19759134<ref>PMID:19759134</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 3iya" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</SX>
</SX>
[[Category: Dengue virus 2]]
[[Category: Dengue virus 2]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Chen, J]]
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[[Category: Chen J]]
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[[Category: Chipman, P R]]
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[[Category: Chipman PR]]
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[[Category: Holdaway, H A]]
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[[Category: Holdaway HA]]
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[[Category: Kuhn, R J]]
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[[Category: Kuhn RJ]]
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[[Category: Rossmann, M G]]
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[[Category: Rossmann MG]]
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[[Category: Yu, I]]
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[[Category: Yu I]]
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[[Category: Icosahedral virus]]
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[[Category: Prm]]
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[[Category: Virus]]
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Current revision

Association of the pr peptides with dengue virus blocks membrane fusion at acidic pH

3iya, resolution 22.00Å

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OCA

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