1g7p
From Proteopedia
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| , resolution 1.50Å | |||||||
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| Ligands: | |||||||
| Activity: | Alpha-glucosidase, with EC number 3.2.1.20 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF MHC CLASS I H-2KB HEAVY CHAIN COMPLEXED WITH BETA-2 MICROGLOBULIN AND YEAST ALPHA-GLUCOSIDASE
Overview
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.
About this Structure
1G7P is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Mar 20 11:19:21 2008
Categories: Alpha-glucosidase | Mus musculus | Protein complex | Apostolopoulos, V. | Corper, A L. | Li, W. | McKenzie, I F. | Teyton, L. | Wilson, I A. | Yu, M. | NAG | H-2kb | Mhc class i | S. cerevisiae | Yeast
