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rdf:type |
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lifeskim:mentions |
umls-concept:C0006933,
umls-concept:C0033684,
umls-concept:C0222679,
umls-concept:C0678594,
umls-concept:C1514562,
umls-concept:C1627932,
umls-concept:C1706853,
umls-concept:C1707271,
umls-concept:C1880389,
umls-concept:C1883204,
umls-concept:C1883221
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pubmed:issue |
2
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pubmed:dateCreated |
2008-12-30
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pubmed:abstractText |
Adenovirus serotype 5 protein IX (pIX) has two domains connected by a flexible linker. Three N-terminal domains form triskelions on the capsid facets that cement hexons together, and the C-terminal domains of four monomers form complexes toward the facet periphery. Here we present a cryoelectron microscopy structure of recombinant adenovirus with a peptide tag added to the C terminus of pIX. The structure, made up by several C termini of pIX, is longer at both ends than the wild-type protein, and Fabs directed against the tag bind to both ends of the oligomer, demonstrating that the pIX C termini associate in an antiparallel manner.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/19004948-11435594,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19004948-15194799,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19004948-15861131,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19004948-15914835,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19004948-17005667,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19004948-17268536,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19004948-17584037,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19004948-18216088,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19004948-1913814,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19004948-2196380,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19004948-8030241,
http://linkedlifedata.com/resource/pubmed/commentcorrection/19004948-8676512
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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 |
Jan
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pubmed:issn |
1098-5514
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
83
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1135-9
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:19004948-Adenoviridae,
pubmed-meshheading:19004948-Antibodies, Viral,
pubmed-meshheading:19004948-Capsid Proteins,
pubmed-meshheading:19004948-Cryoelectron Microscopy,
pubmed-meshheading:19004948-Humans,
pubmed-meshheading:19004948-Models, Molecular,
pubmed-meshheading:19004948-Protein Binding,
pubmed-meshheading:19004948-Protein Structure, Quaternary
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pubmed:year |
2009
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pubmed:articleTitle |
The C-terminal domains of adenovirus serotype 5 protein IX assemble into an antiparallel structure on the facets of the capsid.
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pubmed:affiliation |
Université Joseph Fourier, Unit for Virus Host Cell Interaction, UMR 5233 UJF-EMBL-CNRS, Grenoble cedex 9, France.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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