Linked Life Data

8280703

Source:http://linkedlifedata.com/resource/pubmed/id/8280703

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1994-2-17
pubmed:abstractText
Self-peptide pools eluted from purified H-2Kk or H-2Kkm1 molecules were sequenced. The majority of self-peptides associated with H-2Kk molecules were found to be octamers with two anchor positions. Position 2 is invariantly occupied with Glu, and the C-terminal residue at position 8 is almost always Ile. Comparison of this motif with synthetic peptides known to contain viral or parasite T-cell epitopes could be well aligned with this motif, except that the C-terminal Ile residue frequently appears to be at position 9 of the aligned sequences, instead of 8. Self-peptides eluted from mutant H-2Kkm1 molecules also appear to be mostly octamers with the same Ile residues at position 8 as with Kk. Position 2 is still dominantly occupied by Glu; in contrast to the Kk motif, however, Gln, Gly, and Pro are also allowed. Other differences between the two motifs indicate that a certain number of peptides presented by one of the molecules are not presented by the other.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1067-5582
pubmed:author
pubmed:issnType
Print
pubmed:volume
14
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
144-9
pubmed:dateRevised
2007-5-4
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Comparison of the H-2Kk- and H-2Kkm1-restricted peptide motifs.
pubmed:affiliation
Max-Planck-Institut für Biologie, Abteilung Immungenetik, Tübingen, Germany.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't