IMR Press / FBL / Volume 6 / Issue 3 / DOI: 10.2741/apostol

Frontiers in Bioscience-Landmark (FBL) is published by IMR Press from Volume 26 Issue 5 (2021). Previous articles were published by another publisher on a subscription basis, and they are hosted by IMR Press on as a courtesy and upon agreement with Frontiers in Bioscience.

Getting into the groove: unusual features of peptide binding to MHC class I molecules and implications in vaccine design
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1 The Austin Research Institute, Studley Rd, Heidelberg, VIC, 3084, Australia
2 Department of Molecular Biology and Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 N Torrey Pines Rd (BCC-206), La Jolla, CA, 92037
Front. Biosci. (Landmark Ed) 2001, 6(3), 1311–1320;
Published: 1 October 2001

The major histocompatibility complex presents antigenic peptides on the surface of antigen presenting cells to T cell receptors. Recognition of peptide-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 bind to MHC class I molecules is an important prerequisite in the design of vaccines. Herein, we will discuss, with special emphasis on MUC1, unusual features of MUC1 peptide binding to MHC class I, obtained from vaccine studies including a MUC1 peptide mimic and the crystal structures of low and high affinity peptides lacking canonical anchor motifs in complex with H-2Kb.

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