1tg8
From Proteopedia
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- | [[Image:1tg8.png|left|200px]] | ||
- | + | ==The structure of Dengue virus E glycoprotein== | |
+ | <StructureSection load='1tg8' size='340' side='right'caption='[[1tg8]], [[Resolution|resolution]] 2.61Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[1tg8]] is a 1 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=1TG8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1TG8 FirstGlance]. <br> | ||
+ | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.61Å</td></tr> | ||
+ | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene></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=1tg8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tg8 OCA], [https://pdbe.org/1tg8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1tg8 RCSB], [https://www.ebi.ac.uk/pdbsum/1tg8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1tg8 ProSAT]</span></td></tr> | ||
+ | </table> | ||
+ | == Function == | ||
+ | [https://www.uniprot.org/uniprot/POLG_DEN2T POLG_DEN2T] 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). | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | 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. | ||
- | + | 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:15341726<ref>PMID:15341726</ref> | |
- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | <div class="pdbe-citations 1tg8" style="background-color:#fffaf0;"></div> | |
- | + | == References == | |
- | + | <references/> | |
- | == | + | __TOC__ |
- | < | + | </StructureSection> |
[[Category: Dengue virus 2]] | [[Category: Dengue virus 2]] | ||
- | [[Category: Baker | + | [[Category: Large Structures]] |
- | [[Category: Clements | + | [[Category: Baker TS]] |
- | [[Category: Ogata | + | [[Category: Clements D]] |
- | [[Category: Rossmann | + | [[Category: Ogata S]] |
- | [[Category: Strauss | + | [[Category: Rossmann MG]] |
- | [[Category: Zhang | + | [[Category: Strauss JH]] |
- | [[Category: Zhang | + | [[Category: Zhang W]] |
- | + | [[Category: Zhang Y]] | |
- | + |
Current revision
The structure of Dengue virus E glycoprotein
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Categories: Dengue virus 2 | Large Structures | Baker TS | Clements D | Ogata S | Rossmann MG | Strauss JH | Zhang W | Zhang Y