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4oig

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{{STRUCTURE_4oig| PDB=4oig | SCENE= }}
 
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===Dengue Virus Non-structural Protein NS1===
 
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{{ABSTRACT_PUBMED_24594604}}
 
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==Function==
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==Dengue Virus Non-structural Protein NS1==
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[[http://www.uniprot.org/uniprot/POLG_DEN1W POLG_DEN1W]] 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).
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<StructureSection load='4oig' size='340' side='right'caption='[[4oig]], [[Resolution|resolution]] 2.69&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[4oig]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Dengue_virus_1_Nauru/West_Pac/1974 Dengue virus 1 Nauru/West Pac/1974]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OIG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OIG FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.69&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=4oig FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oig OCA], [https://pdbe.org/4oig PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4oig RCSB], [https://www.ebi.ac.uk/pdbsum/4oig PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4oig ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The Flavivirus nonstructural protein 1 (NS1) is a conserved, membrane-associated and secreted glycoprotein with replication and immune evasion functions. Secreted NS1 is a hexameric, barrel-shaped lipoprotein that can bind back to the plasma membrane of cells. Antibodies targeting cell surface-associated NS1 can be protective in vivo in a manner dependent on Fc effector functions. We describe here the crystal structure of a C-terminal fragment (residues 172-352) of West Nile (WNV) and Dengue virus NS1 proteins at 1.85 and 2.7 A resolution, respectively. NS1172-352 assembles as a unique rod-shaped dimer composed of a 16-stranded beta-platform flanked on one face by protruding connecting loops. We also determined the 3.0 A resolution structure of WNV NS1172-352 with the protective 22NS1 antibody Fab, which engages the loop-face of the rod. The head-to-head NS1172-352 dimer we observe in crystal lattices is supported by multiangle light and small-angle X-ray scattering studies. We used the available cryo-electron microscopy reconstruction to develop a pseudoatomic model of the NS1 hexamer. The model was constructed with the NS1172-352 dimeric rod aligned with the long axis of the barrel, and with the loop-face oriented away from the core. Difference densities suggest that the N-terminal region of NS1 forms globular lobes that mediate lateral contacts between dimers in the hexamer. Our model also suggests that the N-terminal lobe forms the surface of the central cavity where lipid binding may occur.
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==About this Structure==
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Structural basis of Flavivirus NS1 assembly and antibody recognition.,Edeling MA, Diamond MS, Fremont DH Proc Natl Acad Sci U S A. 2014 Mar 4. PMID:24594604<ref>PMID:24594604</ref>
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[[4oig]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OIG OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<ref group="xtra">PMID:024594604</ref><references group="xtra"/><references/>
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</div>
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[[Category: CSGID, Center for Structural Genomics of Infectious Diseases.]]
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<div class="pdbe-citations 4oig" style="background-color:#fffaf0;"></div>
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[[Category: Edeling, M A.]]
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== References ==
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[[Category: Fremont, D H.]]
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<references/>
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[[Category: Center for structural genomics of infectious disease]]
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__TOC__
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[[Category: Csgid]]
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</StructureSection>
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[[Category: Dengue virus]]
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[[Category: Dengue virus 1 Nauru/West Pac/1974]]
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[[Category: Flavivirus viral protein]]
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[[Category: Large Structures]]
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[[Category: Non-structural protein]]
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[[Category: Edeling MA]]
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[[Category: Ns1]]
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[[Category: Fremont DH]]
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[[Category: Structural genomic]]
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[[Category: Viral protein]]
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Current revision

Dengue Virus Non-structural Protein NS1

PDB ID 4oig

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