The interaction of antigenic peptides with the H-2Kd MHC class I molecule
Details
Serval ID
serval:BIB_6E8F2EBF1064
Type
Article: article from journal or magazin.
Publication sub-type
Review (review): journal as complete as possible of one specific subject, written based on exhaustive analyses from published work.
Collection
Publications
Institution
Title
The interaction of antigenic peptides with the H-2Kd MHC class I molecule
Journal
Seminars in Immunology
ISSN
1044-5323 (Print)
Publication state
Published
Issued date
04/1993
Volume
5
Number
2
Pages
95-104
Notes
Journal Article
Research Support, Non-U.S. Gov't
Review --- Old month value: Apr
Research Support, Non-U.S. Gov't
Review --- Old month value: Apr
Abstract
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.
Keywords
Amino Acid Sequence
Animals
Antigens/chemistry/immunology/*metabolism
Binding Sites
H-2 Antigens/chemistry/immunology/*metabolism
Humans
Models, Molecular
Molecular Sequence Data
Peptides/chemistry/immunology/*metabolism
Pubmed
Create date
28/01/2008 12:28
Last modification date
20/08/2019 15:27