Getting into the groove: Unusual features of peptide binding to MHC class I molecules and implications in vaccine design

Citation
V. Apostolopoulos et al., Getting into the groove: Unusual features of peptide binding to MHC class I molecules and implications in vaccine design, FRONT BIOSC, 6, 2001, pp. D1311-D1320
Citations number
64
Categorie Soggetti
Biochemistry & Biophysics
Journal title
FRONTIERS IN BIOSCIENCE
ISSN journal
10939946 → ACNP
Volume
6
Year of publication
2001
Pages
D1311 - D1320
Database
ISI
SICI code
1093-9946(200110)6:<D1311:GITGUF>2.0.ZU;2-H
Abstract
The major histocompatibility complex presents antigenic peptides on the sur face of antigen presenting cells to T cell receptors. Recognition of peptid e-MHC by T cells initiates a cascade of signals in T cells which maintains a T cell dependent immune response. An understanding of the how peptides bi nd to MHC class I molecules is an important prerequisite in the design of v accines. Herein, we will discuss, with special emphasis on MUC1, unusual fe atures of MUC1 peptide binding to MHC class I, obtained from vaccine studie s including a MUC1 peptide mimic and the crystal structures of low and high affinity peptides lacking canonical anchor motifs in complex with H-2K(b).