3miw: Difference between revisions

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 ==Crystal Structure of Rotavirus NSP4==
-<StructureSection load='3miw' size='340' side='right' caption='[[3miw]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
+<StructureSection load='3miw' size='340' side='right'caption='[[3miw]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3miw]] is a 10 chain structure with sequence from [http://en.wikipedia.org/wiki/Rotavirus_g4 Rotavirus g4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MIW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MIW FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3miw]] is a 10 chain structure with sequence from [https://en.wikipedia.org/wiki/Human_rotavirus_G4_strain_St._Thomas_3 Human rotavirus G4 strain St. Thomas 3]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MIW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3MIW FirstGlance]. <br>
-</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene><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]] 2.5&#8491;</td></tr>
-<tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2o1j|2o1j]], [[2o1k|2o1k]]</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=EDO:1,2-ETHANEDIOL'>EDO</scene></td></tr>
-<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">G10 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=35336 Rotavirus G4])</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=3miw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3miw OCA], [https://pdbe.org/3miw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3miw RCSB], [https://www.ebi.ac.uk/pdbsum/3miw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3miw ProSAT]</span></td></tr>
-<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3miw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3miw OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3miw RCSB], [http://www.ebi.ac.uk/pdbsum/3miw PDBsum]</span></td></tr>
+</table>
-<table>
+== Function ==
-<div style="background-color:#fffaf0;">
+[https://www.uniprot.org/uniprot/NSP4_ROTHT NSP4_ROTHT] Involved in virus morphogenesis. Functions as a receptor for the immature double-layered inner capsid particle (ICP) which transiently buds into the lumen of the rough endoplasmic reticulum during viral maturation (By similarity).  Enterotoxin that causes a phospholipase C-dependent elevation of the intracellular calcium concentration in host intestinal mucosa cells. Increased concentration of intracellular calcium disrupts the cytoskeleton and the tight junctions, raising the paracellular permeability. Potentiates chloride ion secretion through a calcium ion-dependent signaling pathway, inducing age-dependent diarrhea. To perform this enterotoxigenic role in vivo, NSP4 is probably released from infected enterocytes in a soluble form capable of diffusing within the intestinal lumen and interacting with the plasma membrane receptors on neighboring epithelial cells. Possible receptors for NSP4 are alpha-1/beta-1 and alpha-2/beta-1 integrin heterodimers (By similarity).
-== Publication Abstract from PubMed ==
-The region spanning residues 95-146 of the rotavirus nonstructural protein NSP4 from the asymptomatic human strain ST3 has been purified and crystallized and diffraction data have been collected to a resolution of 2.6 A. Several attempts to solve the structure by the molecular-replacement method using the available tetrameric structures of this domain were unsuccessful despite a sequence identity of 73% to the already known structures. A more systematic approach with a dimer as the search model led to an unexpected pentameric structure using the program Phaser. The various steps involved in arriving at this molecular-replacement solution, which unravelled a case of subtle variation between different oligomeric states unknown at the time of solving the structure, are presented in this paper.
-A new pentameric structure of rotavirus NSP4 revealed by molecular replacement.,Chacko AR, Jeyakanthan J, Ueno G, Sekar K, Rao CD, Dodson EJ, Suguna K, Read RJ Acta Crystallogr D Biol Crystallogr. 2012 Jan;68(Pt 1):57-61. Epub 2011 Dec 9. PMID:22194333<ref>PMID:22194333</ref>
-From MEDLINEÂ®/PubMedÂ®, a database of the U.S. National Library of Medicine.<br>
-</div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Rotavirus g4]]
+[[Category: Human rotavirus G4 strain St. Thomas 3]]
-[[Category: Chacko, A R.]]
+[[Category: Large Structures]]
-[[Category: Dodson, E J.]]
+[[Category: Chacko AR]]
-[[Category: Rao, D C.]]
+[[Category: Dodson EJ]]
-[[Category: Read, R J.]]
+[[Category: Rao DC]]
-[[Category: Suguna, K.]]
+[[Category: Read RJ]]
-[[Category: Non structural protein]]
+[[Category: Suguna K]]
-[[Category: Nsp4]]
-[[Category: Pentameric coiled coil]]
-[[Category: Rotavirus enterotoxin]]
-[[Category: Viral protein]]
-[[Category: Virulence]]