3qsq
From Proteopedia
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- | [[ | + | ==Crystal structure of the projection domain of the human astrovirus capsid protein== |
+ | <StructureSection load='3qsq' size='340' side='right' caption='[[3qsq]], [[Resolution|resolution]] 1.80Å' scene=''> | ||
+ | == Structural highlights == | ||
+ | <table><tr><td colspan='2'>[[3qsq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human_astrovirus_8 Human astrovirus 8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3QSQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3QSQ FirstGlance]. <br> | ||
+ | </td></tr><tr><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=43358 Human astrovirus 8])</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=3qsq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3qsq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3qsq RCSB], [http://www.ebi.ac.uk/pdbsum/3qsq PDBsum]</span></td></tr> | ||
+ | <table> | ||
+ | <div style="background-color:#fffaf0;"> | ||
+ | == Publication Abstract from PubMed == | ||
+ | Astroviruses are single-stranded, plus-sense RNA viruses that infect both mammals and birds, causing gastroenteritis and other extraintestinal diseases. Clinical studies have established astroviruses as the second leading cause of viral diarrhea in young children. Here we report the crystal structure of the human astrovirus dimeric surface spike determined to 1.8-A resolution. The overall structure of each spike/projection domain has a unique three-layered beta-sandwiches fold, with a core, six-stranded beta-barrel structure that is also found in the hepatitis E virus capsid protrusions, suggesting a closer phylogenetic relationship between these two viruses than previously acknowledged. Based on a hepatitis E virus capsid model, we performed homology modeling and produced a complete, T = 3 astrovirus capsid model with features remarkably similar to those observed in a cryoelectron microscopy reconstruction image of a human astrovirus. Mapping conserved residues onto the astrovirus projection domain revealed a putative receptor binding site with amino acid compositions characteristic for polysaccharide recognition. Our results will have an important impact on future characterization of astrovirus structure and function, and will likely have practical applications in the development of vaccines and antivirals. | ||
- | + | Crystal structure of the human astrovirus capsid spike.,Dong J, Dong L, Mendez E, Tao Y Proc Natl Acad Sci U S A. 2011 Aug 2;108(31):12681-6. Epub 2011 Jul 18. PMID:21768348<ref>PMID:21768348</ref> | |
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- | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
- | + | </div> | |
- | + | == References == | |
- | + | <references/> | |
- | + | __TOC__ | |
- | + | </StructureSection> | |
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[[Category: Human astrovirus 8]] | [[Category: Human astrovirus 8]] | ||
[[Category: Dong, J.]] | [[Category: Dong, J.]] |
Revision as of 04:51, 5 June 2014
Crystal structure of the projection domain of the human astrovirus capsid protein
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