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pubmed-article:19004948pubmed:abstractTextAdenovirus 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.lld:pubmed
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pubmed-article:19004948pubmed:pagination1135-9lld:pubmed
pubmed-article:19004948pubmed:dateRevised2009-11-18lld:pubmed
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pubmed-article:19004948pubmed:year2009lld:pubmed
pubmed-article:19004948pubmed:articleTitleThe C-terminal domains of adenovirus serotype 5 protein IX assemble into an antiparallel structure on the facets of the capsid.lld:pubmed
pubmed-article:19004948pubmed:affiliationUniversité Joseph Fourier, Unit for Virus Host Cell Interaction, UMR 5233 UJF-EMBL-CNRS, Grenoble cedex 9, France.lld:pubmed
pubmed-article:19004948pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:19004948pubmed:publicationTypeResearch Support, Non-U.S. Gov'tlld:pubmed
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