Publications & Reports

Crystal structure of a non-canonical high affinity peptide complexed with MHC class I: a novel use of alternative anchors.

Apostolopoulos V, Yu M, Corper AL, Li W, McKenzie IF, Teyton L, Wilson IA, Plebanski M
Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037, USA. v.apostolopoulos@ari.unimelb.edu.au

Abstract

The crystal structure of a non-standard peptide, YEA9, in complex with H-2Kb, at 1.5 A resolution demonstrates how YEA9 peptide can bind with surprisingly high affinity through insertion of alternative, long, non-canonical anchors into the B and E pockets. The use of “alternative pockets” represents a new mode of high affinity peptide binding, that should be considered when predicting peptide epitopes for MHC class I. These novel interactions encountered in this non-canonical high affinity peptide-MHC complex should help predict additional binding peptides from primary protein sequences and aid in the design of alternative approaches for peptide-based vaccines.

Publication

  • Journal: Journal of Molecular Biology
  • Published: 17/05/2002
  • Volume: 318
  • Issue: 5
  • Pagination: 1307-1316