Linked Life Data

8504219

Source:http://linkedlifedata.com/resource/pubmed/id/8504219

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1993-7-2
pubmed:abstractText
An important event in the recognition of antigen by T cells is the selective interaction of peptides with major histocompatibility complex (MHC) molecules. We have defined several critical structural features that promote the efficient interaction of antigenic peptides with the MHC class I molecule, H-2Kd. For four unrelated antigens, we found that optimal synthetic peptides were short, only 9 or 10 amino acids long. These and other H-2Kd-restricted peptides were found to share a distinct 2-residue binding motif. Two regions in the H-2Kd antigen binding site that might accommodate the motif residues were identified by analysis of Ala-substituted H-2Kd molecules. A molecular model showing the possible interaction of one antigenic peptide with the H-2Kd molecule is presented.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Apr
pubmed:issn
1044-5323
pubmed:author
pubmed:issnType
Print
pubmed:volume
5
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
95-104
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
The interaction of antigenic peptides with the H-2Kd MHC class I molecule.
pubmed:affiliation
Ludwig Institute for Cancer Research, Lausanne Branch, Epalinges, Switzerland.
pubmed:publicationType
Journal Article, Review, Research Support, Non-U.S. Gov't