1eez
From Proteopedia
Crystal Structure Determination of HLA-A2.1 Complexed to GP2 Peptide Variant(I2L/V5L)
Overview
An immunogenic peptide (GP2) derived from HER-2/neu binds to HLA-A2.1 very poorly. Some altered-peptide ligands (APL) of GP2 have increased binding affinity and generate improved cytotoxic T lymphocyte recognition of GP2-presenting tumor cells, but most do not. Increases in binding affinity of single-substitution APL are not additive in double-substitution APL. A common first assumption about peptide binding to class I major histocompatibility complex is that each residue binds independently. In addition, immunologists interested in immunotherapy frequently assume that anchor substitutions do not affect T cell receptor contact residues. However, the crystal structures of two GP2 APL show that the central residues change position depending on the identity of the anchor residue(s). Thus, it is clear that subtle changes in the identity of anchor residues may have significant effects on the positions of the T cell receptor contact residues.
About this Structure
1EEZ is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Class I major histocompatibility complex anchor substitutions alter the conformation of T cell receptor contacts., Sharma AK, Kuhns JJ, Yan S, Friedline RH, Long B, Tisch R, Collins EJ, J Biol Chem. 2001 Jun 15;276(24):21443-9. Epub 2001 Apr 3. PMID:11287414 Page seeded by OCA on Fri May 2 15:01:00 2008
