Linked Life Data

12627395

Source:http://linkedlifedata.com/resource/pubmed/id/12627395

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2003-3-10
pubmed:abstractText
The crystal structure of the reovirus attachment protein, sigma1, reveals a fibre-like structure that is remarkably similar to that of the adenovirus attachment protein, fibre. Both proteins are trimers with head-and-tail morphology. They share unique domain structures and functional properties including defined regions of flexibility within the tail and an unusual symmetry mismatch with the pentameric viral capsid protein into which they are inserted. Moreover, the receptors for reoviruses and adenoviruses, junctional adhesion molecule 1 and coxsackievirus and adenovirus receptor, respectively, also share key structural and functional properties. Although reoviruses and adenoviruses belong to different virus families and have few properties in common, the observed similarities between sigma1 and fibre point to a conserved mechanism of attachment and an ancient evolutionary relationship.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
1052-9276
pubmed:author
pubmed:copyrightInfo
Copyright 2003 John Wiley & Sons, Ltd.
pubmed:issnType
Print
pubmed:volume
13
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
123-32
pubmed:dateRevised
2011-7-1
pubmed:meshHeading
pubmed:articleTitle
Structural evidence for common functions and ancestry of the reovirus and adenovirus attachment proteins.
pubmed:affiliation
Laboratory of Developmental Immunology and Renal Unit, Massachusetts General Hospital, Harvard Medical School, Boston, MA 02114, USA. tstehle@partners.org
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Review, Research Support, Non-U.S. Gov't