Source:http://linkedlifedata.com/resource/pubmed/id/11024472
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
3
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pubmed:dateCreated |
2000-10-23
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pubmed:abstractText |
Icosahedral virus-like particles (VLPs) of RNA phage Qbeta are stabilized by four disulfide bonds of cysteine residues 74 and 80 within the loop between beta-strands F and G (FG loop) of the monomeric subunits, which determine the five-fold and quasi-six-fold symmetry contacts of the VLPs. In order to reduce the stability of Qbeta VLPs, we mutationally converted the amino acid stretch 76-ANGSCD-81 within the FG loop into the 76-VGGVEL-81 sequence. It led to production in Escherichia coli cells of aberrant rod-like Qbeta VLPs, along with normal icosahedral capsids. The length of the rod-like particles exceeded 4-30 times the diameter of icosahedral Qbeta VLPs.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0014-5793
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
6
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pubmed:volume |
482
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
261-4
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11024472-Allolevivirus,
pubmed-meshheading:11024472-Amino Acid Sequence,
pubmed-meshheading:11024472-Cysteine,
pubmed-meshheading:11024472-Genetic Vectors,
pubmed-meshheading:11024472-Molecular Sequence Data,
pubmed-meshheading:11024472-Mutagenesis, Site-Directed,
pubmed-meshheading:11024472-RNA, Viral,
pubmed-meshheading:11024472-Sequence Homology, Amino Acid,
pubmed-meshheading:11024472-Virion
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pubmed:year |
2000
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pubmed:articleTitle |
Mutilation of RNA phage Qbeta virus-like particles: from icosahedrons to rods.
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pubmed:affiliation |
Biomedical Research and Study Centre, University of Latvia, 1 Ratsupites Street, LV-1067, Riga, Latvia.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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