Crystal structure of a non-canonical high affinity peptide complexed with MHC class I: a novel use of alternative anchors |
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Authors: | Apostolopoulos Vasso Yu Minmin Corper Adam L Li Wenjun McKenzie Ian F C Teyton Luc Wilson Ian A Plebanski Magdalena |
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Affiliation: | Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037, USA. v.apostolopoulos@ari.unimelb.edu.au |
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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. |
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Keywords: | MHC class I non-canonical anchor motif peptides YEA9 vaccine design H-2Kb |
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