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rdf:type |
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lifeskim:mentions |
umls-concept:C0162332,
umls-concept:C0242808,
umls-concept:C0597358,
umls-concept:C0597705,
umls-concept:C0678594,
umls-concept:C1514562,
umls-concept:C1643392,
umls-concept:C1706089,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221,
umls-concept:C2709163
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pubmed:issue |
11
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pubmed:dateCreated |
2010-5-5
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pubmed:abstractText |
Our previous structural studies on intact, infectious murine norovirus 1 (MNV-1) virions demonstrated that the receptor binding protruding (P) domains are lifted off the inner shell of the virus. Here, the three-dimensional (3D) reconstructions of recombinant rabbit hemorrhagic disease virus (rRHDV) virus-like particles (VLPs) and intact MNV-1 were determined to approximately 8-A resolution. rRHDV also has a raised P domain, and therefore, this conformation is independent of infectivity and genus. The atomic structure of the MNV-1 P domain was used to interpret the MNV-1 reconstruction. Connections between the P and shell domains and between the floating P domains were modeled. This observed P-domain flexibility likely facilitates virus-host receptor interactions.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
1098-5514
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pubmed:author |
pubmed-author:CavazzaTommasoT,
pubmed-author:KatpallyUmeshU,
pubmed-author:RubinJohn RJR,
pubmed-author:SmithThomas JTJ,
pubmed-author:StuckeyJeanneJ,
pubmed-author:TaubeStefanS,
pubmed-author:VirginHerbert WHW4th,
pubmed-author:VossNeil RNR,
pubmed-author:WardVernon KVK,
pubmed-author:WobusChristiane ECE,
pubmed-author:YoungVivienne LVL
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pubmed:issnType |
Electronic
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pubmed:volume |
84
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
5836-41
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pubmed:dateRevised |
2011-3-3
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pubmed:meshHeading |
pubmed-meshheading:20335264-Animals,
pubmed-meshheading:20335264-Binding Sites,
pubmed-meshheading:20335264-Cryoelectron Microscopy,
pubmed-meshheading:20335264-Hemorrhagic Disease Virus, Rabbit,
pubmed-meshheading:20335264-Imaging, Three-Dimensional,
pubmed-meshheading:20335264-Mice,
pubmed-meshheading:20335264-Norovirus,
pubmed-meshheading:20335264-Pliability,
pubmed-meshheading:20335264-Protein Conformation,
pubmed-meshheading:20335264-Rabbits,
pubmed-meshheading:20335264-Receptors, Virus
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pubmed:year |
2010
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pubmed:articleTitle |
High-resolution cryo-electron microscopy structures of murine norovirus 1 and rabbit hemorrhagic disease virus reveal marked flexibility in the receptor binding domains.
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pubmed:affiliation |
Donald Danforth Plant Science Center, 975 North Warson Road, Saint Louis, MO 63132, USA.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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