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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
6
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pubmed:dateCreated |
2004-3-1
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pubmed:abstractText |
The core protein P3 of Rice dwarf virus constructs asymmetric dimers, one of which is inserted by the amino-terminal region of another P3 protein. The P3 proteins with serial amino-terminal deletions, expressed in a baculovirus system, formed particles with gradually decreasing stability. The capacity for self-assembly disappeared when 52 of the amino-terminal amino acids had been deleted. These results demonstrated that insertion of the amino-terminal arm of one P3 protein into another appears to play an important role in stabilizing the core particles.
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pubmed:commentsCorrections |
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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 |
Mar
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pubmed:issn |
0022-538X
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
78
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
3145-8
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:14990734-Animals,
pubmed-meshheading:14990734-Capsid Proteins,
pubmed-meshheading:14990734-Cell Line,
pubmed-meshheading:14990734-Dimerization,
pubmed-meshheading:14990734-Gene Deletion,
pubmed-meshheading:14990734-Models, Molecular,
pubmed-meshheading:14990734-Nucleopolyhedrovirus,
pubmed-meshheading:14990734-Oryza sativa,
pubmed-meshheading:14990734-Reoviridae,
pubmed-meshheading:14990734-Structure-Activity Relationship,
pubmed-meshheading:14990734-Virion,
pubmed-meshheading:14990734-Virus Assembly
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pubmed:year |
2004
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pubmed:articleTitle |
The amino-terminal region of major capsid protein P3 is essential for self-assembly of single-shelled core-like particles of Rice dwarf virus.
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pubmed:affiliation |
Laboratory of Virology, National Agricultural Research Center, Tsukuba, Ibaraki 305-8666, Japan.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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