1g7p: Difference between revisions
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'''CRYSTAL STRUCTURE OF MHC CLASS I H-2KB HEAVY CHAIN COMPLEXED WITH BETA-2 MICROGLOBULIN AND YEAST ALPHA-GLUCOSIDASE''' | '''CRYSTAL STRUCTURE OF MHC CLASS I H-2KB HEAVY CHAIN COMPLEXED WITH BETA-2 MICROGLOBULIN AND YEAST ALPHA-GLUCOSIDASE''' | ||
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[[Category: Wilson, I A.]] | [[Category: Wilson, I A.]] | ||
[[Category: Yu, M.]] | [[Category: Yu, M.]] | ||
[[Category: | [[Category: Alpha-glucosidase]] | ||
[[Category: | [[Category: H-2kb]] | ||
[[Category: | [[Category: Mhc class i]] | ||
[[Category: | [[Category: S. cerevisiae]] | ||
[[Category: | [[Category: Yeast]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:14:40 2008'' | |||
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Revision as of 14:14, 2 May 2008
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 Fri May 2 17:14:40 2008
