Competitor analogs for defined T cell antigens: peptides incorporating a putative binding motif and polyproline or polyglycine spacers
Details
Serval ID
serval:BIB_9B5193EABEA2
Type
Article: article from journal or magazin.
Collection
Publications
Institution
Title
Competitor analogs for defined T cell antigens: peptides incorporating a putative binding motif and polyproline or polyglycine spacers
Journal
Cell
ISSN
0092-8674 (Print)
Publication state
Published
Issued date
01/1990
Volume
60
Number
1
Pages
63-72
Notes
Journal Article
Research Support, Non-U.S. Gov't --- Old month value: Jan 12
Research Support, Non-U.S. Gov't --- Old month value: Jan 12
Abstract
We describe a new approach for modeling antigenic peptides recognized by T cells. Peptide A24 170-182 can compete with other antigenic peptides that are recognized by H-2kd-restricted cytolytic T cells, presumably by binding to the Kd molecule. By comparing substituted A24 peptides as competitors in a functional competition assay, the A24 residues Tyr-171, Thr-178, and Leu-179 were identified as possible contact residues for Kd. A highly active competitor peptide analog was synthesized in which Tyr was separated from the Thr-Leu pair by a pentaproline spacer. The choice of proline allowed the prediction of a probable conformation for the analog when bound to the Kd molecule. The simplest conformation of the A24 peptide that allows the same spacing and orientation of the motif as in the analog would be a nearly extended polypeptide chain incorporating a single 3(10) helical turn or similar structural kink.
Keywords
Amino Acid Sequence
Animals
Binding, Competitive
Cells, Cultured
Clone Cells
Cytotoxicity, Immunologic
*Glycine
HLA Antigens/*immunology
Major Histocompatibility Complex
Mice
Mice, Inbred DBA
Models, Molecular
Molecular Sequence Data
Oligopeptides/chemical synthesis/immunology/*pharmacology
*Proline
Protein Conformation
Structure-Activity Relationship
T-Lymphocytes, Cytotoxic/*immunology
Pubmed
Web of science
Create date
24/01/2008 15:55
Last modification date
20/08/2019 16:02