Linked Life Data

7796669

Source:http://linkedlifedata.com/resource/pubmed/id/7796669

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1995-8-3
pubmed:abstractText
Peptides that are presented to T-cells by class I major histocompatibility complex molecules are derived from cytosolic proteins. They are generated in the cytosol and translocated into the endoplasmic reticulum (ER) by the transporters associated with antigen processing (TAP molecules). Competition experiments suggest that TAP molecules can specifically translocate a wide range of peptides from 8-13 amino acids long; longer peptides are less likely to be transported. A photoactivatable peptide derivative has been used to demonstrate that competition for transport into the ER reflects competition for a specific peptide-binding site on the TAP molecule. Class I molecules bind the translocated peptides in the ER thereby allowing their transport to the cell surface. The assembly of the class I-peptide complex in the ER is tightly regulated. The evidence suggests that class I heavy chains first dimerize with beta 2-microglobulin in a process mediated by the chaperone calnexin. The class I-beta 2-microglobulin dimer then physically associates with TAP molecules and is released for transport when it binds a peptide.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0300-5208
pubmed:author
pubmed:issnType
Print
pubmed:volume
187
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
150-62; discussion 162-9
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
1994
pubmed:articleTitle
Assembly and transport of class I MHC-peptide complexes.
pubmed:affiliation
Section of Immunobiology, Howard Hughes Medical Institute, Yale University School of Medicine, New Haven, CT 06510, USA.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't