3ts3: Difference between revisions

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 ==Crystal structure of the projection domain of the turkey astrovirus capsid protein at 1.5 angstrom resolution==
-<StructureSection load='3ts3' size='340' side='right' caption='[[3ts3]], [[Resolution|resolution]] 1.49&Aring;' scene=''>
+<StructureSection load='3ts3' size='340' side='right'caption='[[3ts3]], [[Resolution|resolution]] 1.49&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[3ts3]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Tasv2 Tasv2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TS3 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TS3 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[3ts3]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Turkey_astrovirus_2 Turkey astrovirus 2]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TS3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TS3 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.49&#8491;</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">ORF2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=246343 TASV2])</td></tr>
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ts3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ts3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ts3 RCSB], [http://www.ebi.ac.uk/pdbsum/3ts3 PDBsum]</span></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=3ts3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ts3 OCA], [https://pdbe.org/3ts3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3ts3 RCSB], [https://www.ebi.ac.uk/pdbsum/3ts3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3ts3 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CAPSD_TASV2 CAPSD_TASV2]] Capsid polyprotein VP90: self-assembles to form an icosahedral T=3 capsid (By similarity).
+[https://www.uniprot.org/uniprot/CAPSD_TASV2 CAPSD_TASV2] Capsid polyprotein VP90: self-assembles to form an icosahedral T=3 capsid (By similarity).
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-Astroviruses are small, nonenveloped, single-stranded RNA viruses that cause diarrhea in a wide variety of mammals and birds. On the surface of the viral capsid are globular spikes that are thought to be involved in attachment to host cells. To understand the basis of species specificity, we investigated the structure of an avian astrovirus capsid spike and compared it to a previously reported human astrovirus capsid spike structure. Here we report the crystal structure of the turkey astrovirus 2 (TAstV-2) capsid surface spike domain, determined to 1.5-A resolution, and identify three conserved patches on the surface of the spike that are candidate avian receptor-binding sites. Surprisingly, the overall TAstV-2 capsid spike structure is unique, with only distant structural similarities to the human astrovirus capsid spike and other viral capsid spikes. There is an absence of conserved putative receptor-binding sites between the human and avian spikes. However, there is evidence for carbohydrate-binding sites in both human and avian spikes, and studies with human astrovirus 1 (HAstV-1) suggest a minor role in infection for chondroitin sulfate but not heparin. Overall, our structural and functional studies provide new insights into astrovirus host cell entry, species specificity, and evolution.
-Crystal structure of the avian astrovirus capsid spike.,DuBois RM, Freiden P, Marvin S, Reddivari M, Heath RJ, White SW, Schultz-Cherry S J Virol. 2013 Jul;87(14):7853-63. doi: 10.1128/JVI.03139-12. Epub 2013 May 8. PMID:23658448<ref>PMID:23658448</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Tasv2]]
+[[Category: Large Structures]]
-[[Category: DuBois, R M]]
+[[Category: Turkey astrovirus 2]]
-[[Category: Schultz-Cherry, S]]
+[[Category: DuBois RM]]
-[[Category: White, S W]]
+[[Category: Schultz-Cherry S]]
-[[Category: Astrovirus capsid]]
+[[Category: White SW]]
-[[Category: Projection domain]]
-[[Category: Viral protein]]
-[[Category: Virus protein]]