1G7P

CRYSTAL STRUCTURE OF MHC CLASS I H-2KB HEAVY CHAIN COMPLEXED WITH BETA-2 MICROGLOBULIN AND YEAST ALPHA-GLUCOSIDASE

Summary for 1G7P

• Entry DOI: 10.2210/pdb1g7p/pdb
• Related: 1VAD 2VAB
• Descriptor: H-2 CLASS I HISTOCOMPATIBILITY ANTIGEN, K-B ALPHA CHAIN, BETA-2 MICROGLOBULIN, ALPHA-GLUCOSIDASE P1, ... (6 entities in total)
• Functional Keywords: mhc class i, h-2kb, yeast, s. cerevisiae, alpha-glucosidase, immune system
• Biological source: Mus musculus (house mouse); More
• Total number of polymer chains: 3
• Total formula weight: 45233.64

Authors

Apostolopoulos, V.,Yu, M.,Corper, A.L.,Li, W.,McKenzie, I.F.,Teyton, L.,Wilson, I.A. (deposition date: 2000-11-13, release date: 2002-07-17, Last modification date: 2024-10-30)

Primary citation

Apostolopoulos, V.,Yu, M.,Corper, A.L.,Li, W.,McKenzie, I.F.,Teyton, L.,Wilson, I.A.
Crystal structure of a non-canonical high affinity peptide complexed with MHC class I: a novel use of alternative anchors.
J.Mol.Biol., 318:1307-1316, 2002

PubMed 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.

PubMed: 12083519
DOI: 10.1016/S0022-2836(02)00198-5

Experimental method

X-RAY DIFFRACTION (1.5 Å)