4oig: Difference between revisions

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'''Unreleased structure'''


The entry 4oig is ON HOLD
==Dengue Virus Non-structural Protein NS1==
<StructureSection load='4oig' size='340' side='right'caption='[[4oig]], [[Resolution|resolution]] 2.69&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
<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>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


Authors: Edeling, M.A., Fremont, D.H., Center for Structural Genomics of Infectious Diseases (CSGID)
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>


Description: Dengue Virus Non-structural Protein NS1
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4oig" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Dengue virus 1 Nauru/West Pac/1974]]
[[Category: Large Structures]]
[[Category: Edeling MA]]
[[Category: Fremont DH]]