Linked Life Data

1887593

Source:http://linkedlifedata.com/resource/pubmed/id/1887593

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1991-10-9
pubmed:abstractText
The implications of reovirus sigma l protein trimerization on its cell-binding function were investigated. Both monomeric and trimeric forms of sigma l were found to be present when full-length type 3 reovirus Sl transcripts prepared in vitro were translated in rabbit reticulocyte lysates. Pulse-chase experiments demonstrated that monomers were precursors of trimers. However, only the trimeric form was capable of binding to cell surface receptors. Protease and antibody recognition analyses revealed significant structural differences between these two sigma l forms at both the N- and C-termini. Our results suggest that trimerization of protein sigma l is accompanied by extensive conformational changes necessary for its cell attachment function.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0042-6822
pubmed:author
pubmed:issnType
Print
pubmed:volume
184
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
758-61
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1991
pubmed:articleTitle
Trimerization of the reovirus cell attachment protein (sigma 1) induces conformational changes in sigma 1 necessary for its cell-binding function.
pubmed:affiliation
Department of Microbiology and Infectious Diseases, University of Calgary Health Sciences Centre, Alberta, Canada.
pubmed:publicationType
Journal Article, In Vitro, Research Support, Non-U.S. Gov't