1eez

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Revision as of 14:36, 12 November 2007

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spinqualitylabelsall models 1eez, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal Structure Determination of HLA-A2.1 Complexed to GP2 Peptide Variant(I2L/V5L)

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

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.

Disease

Known diseases associated with this structure: Abacavir hypersensitivity, susceptibility to OMIM:[142800], Ankylosing spondylitis, susceptibility to, 1 OMIM:[142800], Hypoproteinemia, hypercatabolic OMIM:[109700], Stevens-Johnson syndrome, susceptibility to OMIM:[142800]

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

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