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New page: left|200px<br /><applet load="1thd" size="450" color="white" frame="true" align="right" spinBox="true" caption="1thd" /> '''COMPLEX ORGANIZATION OF DENGUE VIRUS E PROTE...
 
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[[Image:1thd.gif|left|200px]]<br /><applet load="1thd" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1thd" />
'''COMPLEX ORGANIZATION OF DENGUE VIRUS E PROTEIN AS REVEALED BY 9.5 ANGSTROM CRYO-EM RECONSTRUCTION'''<br />


==Overview==
==COMPLEX ORGANIZATION OF DENGUE VIRUS E PROTEIN AS REVEALED BY 9.5 ANGSTROM CRYO-EM RECONSTRUCTION==
Dengue virus, a member of the Flaviviridae family, has a surface composed, of 180 copies each of the envelope (E) glycoprotein and the membrane (M), protein. The crystal structure of an N-terminal fragment of E has been, determined and compared with a previously described structure. The primary, difference between these structures is a 10 degrees rotation about a hinge, relating the fusion domain DII to domains DI and DIII. These two rigid, body components were used for independent fitting of E into the, cryo-electron microscopy maps of both immature and mature dengue viruses., The fitted E structures in these two particles showed a difference of 27, degrees between the two components. Comparison of the E structure in its, postfusion state with that in the immature and mature virions shows a, rotation approximately around the same hinge. Flexibility of E is, apparently a functional requirement for assembly and infection of, flaviviruses.
<SX load='1thd' size='340' side='right' viewer='molstar' caption='[[1thd]], [[Resolution|resolution]] 9.50&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1thd]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Dengue_virus_2_Puerto_Rico/PR159-S1/1969 Dengue virus 2 Puerto Rico/PR159-S1/1969]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1THD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1THD FirstGlance]. <br>
1THD is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Dengue_virus_type_3 Dengue virus type 3]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1THD OCA].  
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 9.5&#8491;</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=1thd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1thd OCA], [https://pdbe.org/1thd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1thd RCSB], [https://www.ebi.ac.uk/pdbsum/1thd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1thd ProSAT]</span></td></tr>
==Reference==
</table>
Conformational changes of the flavivirus E glycoprotein., Zhang Y, Zhang W, Ogata S, Clements D, Strauss JH, Baker TS, Kuhn RJ, Rossmann MG, Structure. 2004 Sep;12(9):1607-18. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15341726 15341726]
== Function ==
[[Category: Dengue virus type 3]]
[https://www.uniprot.org/uniprot/POLG_DEN2P POLG_DEN2P] 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. 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). Non-structural protein 2A may be involved viral RNA replication and capsid assembly (Potential).  Non-structural protein 2B is a required cofactor for the serine protease function of NS3 (By similarity).  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).  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).  Peptide 2k functions as a signal peptide for NS4B and is required for the interferon antagonism activity of the latter (By similarity).  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 (By similarity).  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).
[[Category: Single protein]]
__TOC__
[[Category: Baker, T.S.]]
</SX>
[[Category: Clements, D.]]
[[Category: Dengue virus 2 Puerto Rico/PR159-S1/1969]]
[[Category: Kuhn, R.J.]]
[[Category: Large Structures]]
[[Category: Ogata, S.]]
[[Category: Baker TS]]
[[Category: Rossmann, M.G.]]
[[Category: Clements D]]
[[Category: Strauss, J.H.]]
[[Category: Kuhn RJ]]
[[Category: Zhang, W.]]
[[Category: Ogata S]]
[[Category: Zhang, Y.]]
[[Category: Rossmann MG]]
[[Category: cryo-electron microscopy]]
[[Category: Strauss JH]]
[[Category: cryo-em]]
[[Category: Zhang W]]
[[Category: dengue virus]]
[[Category: Zhang Y]]
[[Category: flaviviridae]]
[[Category: flavivirus]]
[[Category: glycoprotein e]]
[[Category: icosahedral virus]]
 
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Retrieved from "https://proteopedia.org/1thd"