Structural highlights
Function
HA1B_MOUSE Involved in the presentation of foreign antigens to the immune system.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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 J Mol Biol. 2002 May 17;318(5):1307-16. PMID:12083519[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Apostolopoulos V, Yu M, Corper AL, Li W, McKenzie IF, Teyton L, Wilson IA, Plebanski M. Crystal structure of a non-canonical high affinity peptide complexed with MHC class I: a novel use of alternative anchors. J Mol Biol. 2002 May 17;318(5):1307-16. PMID:12083519
