Publication Date:
1995-07-14
Description:
CD1 molecules are distantly related to the major histocompatibility complex (MHC) class I proteins. They are of unknown function. Screening random peptide phage display libraries with soluble empty mouse CD1 (mCD1) identified a peptide binding motif. It consists of three anchor positions occupied by aromatic or bulky hydrophobic amino acids. Equilibrium binding studies demonstrated that mCD1 binds peptides containing the appropriate motif with relatively high affinity. However, in contrast to classical MHC class I molecules, strong binding to mCD1 required relatively long peptides. Peptide-specific, mCD1-restricted T cell responses can be raised, which suggests that the findings are of immunological significance.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Castano, A R -- Tangri, S -- Miller, J E -- Holcombe, H R -- Jackson, M R -- Huse, W D -- Kronenberg, M -- Peterson, P A -- New York, N.Y. -- Science. 1995 Jul 14;269(5221):223-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7542403" target="_blank"〉PubMed〈/a〉
Keywords:
Amino Acid Sequence
;
Animals
;
*Antigen Presentation
;
Antigens, CD/chemistry/*immunology/metabolism
;
Antigens, CD1
;
Cell Line
;
Mice
;
Mice, Inbred C57BL
;
Molecular Sequence Data
;
Peptides/chemistry/*immunology/metabolism
;
T-Lymphocytes, Cytotoxic/*immunology
;
Transfection
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
