5ca6: Difference between revisions
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==Crystallographic structure of apo porcine rotavirus TFR-41 VP8*== | |||
<StructureSection load='5ca6' size='340' side='right'caption='[[5ca6]], [[Resolution|resolution]] 1.90Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[5ca6]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Porcine_rotavirus_serotype_5/strain_TFR-41 Porcine rotavirus serotype 5/strain TFR-41]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5CA6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5CA6 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]] 1.9Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FMT:FORMIC+ACID'>FMT</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=PLM:PALMITIC+ACID'>PLM</scene>, <scene name='pdbligand=VCA:VACCENIC+ACID'>VCA</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=5ca6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ca6 OCA], [https://pdbe.org/5ca6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ca6 RCSB], [https://www.ebi.ac.uk/pdbsum/5ca6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ca6 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/A0A1A9TAH8_ROTP6 A0A1A9TAH8_ROTP6] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Rotavirus-cell binding is the essential first step in rotavirus infection. This binding is a major determinant of rotavirus tropism, as host cell invasion is necessary to initiate infection. Initial rotavirus-cell interactions are mediated by carbohydrate-recognizing domain VP8* of the rotavirus capsid spike protein VP4. Here, we report the first observation of significant structural rearrangement of VP8* from human and animal rotavirus strains upon glycan receptor binding. The structural adaptability of rotavirus VP8* delivers important insights into how human and animal rotaviruses utilize the wider range of cellular glycans identified as VP8* binding partners. Furthermore, our studies on rotaviruses with atypical genetic makeup provide information expected to be critical for understanding the mechanisms of animal rotavirus gene emergence in humans and support implementation of epidemiologic surveillance of animal reservoirs as well as future vaccination schemes. | |||
Substantial Receptor-induced Structural Rearrangement of Rotavirus VP8*: Potential Implications for Cross-Species Infection.,Yu X, Mishra R, Holloway G, von Itzstein M, Coulson BS, Blanchard H Chembiochem. 2015 Oct 12;16(15):2176-81. doi: 10.1002/cbic.201500360. Epub 2015, Sep 3. PMID:26250751<ref>PMID:26250751</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
<div class="pdbe-citations 5ca6" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Porcine rotavirus serotype 5/strain TFR-41]] | |||
[[Category: Blanchard H]] | |||
[[Category: Yu X]] | |||
Latest revision as of 11:36, 27 September 2023
Crystallographic structure of apo porcine rotavirus TFR-41 VP8*Crystallographic structure of apo porcine rotavirus TFR-41 VP8*
Structural highlights
FunctionPublication Abstract from PubMedRotavirus-cell binding is the essential first step in rotavirus infection. This binding is a major determinant of rotavirus tropism, as host cell invasion is necessary to initiate infection. Initial rotavirus-cell interactions are mediated by carbohydrate-recognizing domain VP8* of the rotavirus capsid spike protein VP4. Here, we report the first observation of significant structural rearrangement of VP8* from human and animal rotavirus strains upon glycan receptor binding. The structural adaptability of rotavirus VP8* delivers important insights into how human and animal rotaviruses utilize the wider range of cellular glycans identified as VP8* binding partners. Furthermore, our studies on rotaviruses with atypical genetic makeup provide information expected to be critical for understanding the mechanisms of animal rotavirus gene emergence in humans and support implementation of epidemiologic surveillance of animal reservoirs as well as future vaccination schemes. Substantial Receptor-induced Structural Rearrangement of Rotavirus VP8*: Potential Implications for Cross-Species Infection.,Yu X, Mishra R, Holloway G, von Itzstein M, Coulson BS, Blanchard H Chembiochem. 2015 Oct 12;16(15):2176-81. doi: 10.1002/cbic.201500360. Epub 2015, Sep 3. PMID:26250751[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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