Linked Life Data

9888806

Source:http://linkedlifedata.com/resource/pubmed/id/9888806

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1999-2-16
pubmed:abstractText
The interaction of the receptor-binding domain (R domain) of diphtheria toxin with a pure lipid membrane has been characterized by several approaches. Using a photoactivatable lipid, the R domain has been shown to deeply insert in the lipid membrane. Three regions of the R domain (residues 380-421, 422-441, and 442 to about 483) are protected by their interaction with the membrane from externally added proteases. At least one of these regions is deeply interacting with the lipid membrane, as evidenced by the location of Cys 461 and 471 determined by fluorescence experiments. Binding of the R domain to the lipid membrane is characterized by the appearance of an alpha-helical component whose orientation is compatible with a transmembrane orientation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
0006-2960
pubmed:author
pubmed:issnType
Print
pubmed:day
12
pubmed:volume
38
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
660-6
pubmed:dateRevised
2007-11-15
pubmed:meshHeading
pubmed:year
1999
pubmed:articleTitle
Structure and topology of diphtheria toxin R domain in lipid membranes.
pubmed:affiliation
Laboratoire de Chimie Physique des Macromolécules aux Interfaces, CP 206/2, Université Libre de Bruxelles, Belgium.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't