Linked Life Data

7889401

Source:http://linkedlifedata.com/resource/pubmed/id/7889401

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
1995-4-20
pubmed:abstractText
The peptide selectivity of the human transporters associated with antigen processing (TAP) was investigated using a panel of peptides of varying length and sequence. Peptides were assayed for their ability to compete for the translocation of a labeled reporter peptide containing an N-linked glycosylation acceptor site in Streptolysin O (SLO)-permeabilized cells. We find that human TAP is very promiscuous for peptides in the 8-12 amino acid range, while showing increased selectivity and lower translocation efficiency for peptides in the 13-30 amino acid range. The minimum peptide length appears to be 8 amino acids, while the maximum length appears to be approximately 25 amino acids. Furthermore, a photoactive peptide analogue was synthesized that can photolabel TAP molecules. Using this analogue, we showed that an ATP-independent peptide-binding site exists on TAP, and that competition for translocation reflects competition for peptide binding.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1074-7613
pubmed:author
pubmed:issnType
Print
pubmed:volume
1
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
7-14
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Human transporters associated with antigen processing possess a promiscuous peptide-binding site.
pubmed:affiliation
Section of Immunobiology, Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, Connecticut 06510.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't