Linked Life Data

12747555

Source:http://linkedlifedata.com/resource/pubmed/id/12747555

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
2003-5-15
pubmed:abstractText
Representative adenoviruses from four of the five major virus subgroups have been shown to interact with the 46-kDa coxsackievirus and adenovirus receptor (CAR) that is widely expressed on many human cell types, suggesting that the ability to bind CAR may be a conserved feature of many of the approximately 50 known adenovirus serotypes. Receptor binding is a function of the distal 'knob' domain of the trimeric viral fiber protein. Here we review recent structural characterizations of knob, CAR and knob-CAR complexes, and we discuss how knob architecture may have evolved to accommodate opposing selective pressures to vary antigenic structure while conserving receptor binding specificity. In contrast to the hypervariability of the solvent-exposed surface of knob, the CAR receptor was found to be non-polymorphic.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0070-217X
pubmed:author
pubmed:issnType
Print
pubmed:volume
272
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
331-64
pubmed:dateRevised
2011-7-1
pubmed:meshHeading
pubmed:year
2003
pubmed:articleTitle
Adenovirus interaction with its cellular receptor CAR.
pubmed:affiliation
Biology Department, Brookhaven National Laboratory, Upton, NY 11973, USA.
pubmed:publicationType
Journal Article, Review