Linked Life Data

20017190

Source:http://linkedlifedata.com/resource/pubmed/id/20017190

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2010-1-4
pubmed:abstractText
The endoplasmic reticulum (ER) protein tapasin is essential for the loading of high-affinity peptides onto MHC class I molecules. It mediates peptide editing, i.e. the binding of peptides of successively higher affinity until class I molecules pass ER quality control and exit to the cell surface. The molecular mechanism of action of tapasin is unknown. We describe here the reconstitution of tapasin-mediated peptide editing on class I molecules in the lumen of microsomal membranes. We find that in a competitive situation between high- and low-affinity peptides, tapasin mediates the binding of the high-affinity peptide to class I by accelerating the dissociation of the peptide from an unstable intermediate of the binding reaction.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
1521-4141
pubmed:author
pubmed:issnType
Electronic
pubmed:volume
40
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
214-24
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
Tapasin edits peptides on MHC class I molecules by accelerating peptide exchange.
pubmed:affiliation
Biochemistry and Cell Biology, Jacobs University Bremen, Bremen, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't