Crystal structure of a non-canonical high affinity peptide complexed with MHC class I: a novel use of alternative anchors.
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.
Apostolopoulos
Vasso
V
Department of Molecular Biology, The Scripps Research Institute, La Jolla, CA 92037, USA. v.apostolopoulos@ari.unimelb.edu.au
Yu
Minmin
M
Corper
Adam L
AL
Li
Wenjun
W
McKenzie
Ian F C
IF
Teyton
Luc
L
Wilson
Ian A
IA
Plebanski
Magdalena
M
D000818:Animals; D017951:Antigen Presentation; D004330:Drosophila; D015195:Drug Design; D005656:Fungal Proteins / Q000737:chemistry / Q000276:immunology; D015395:Histocompatibility Antigens Class I / Q000737:chemistry* / Q000276:immunology; D008958:Models, Molecular; D010455:Peptides / Q000737:chemistry* / Q000276:immunology; D011485:Protein Binding; D011487:Protein Conformation; D014612:Vaccines
D005656:Fungal Proteins; D015395:Histocompatibility Antigens Class I; D010455:Peptides; D014612:Vaccines