1i8i

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Revision as of 07:25, 18 November 2007

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spinqualitylabelsall models 1i8i, resolution 2.4Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF DSFV MR1 IN COMPLEX WITH THE PEPTIDE ANTIGEN OF THE MUTANT EPIDERMAL GROWTH FACTOR RECEPTOR, EGFRVIII, AT ROOM TEMPERATURE

Overview

Epitope mapping studies and the determination of the structure to 1.8 A, resolution have been carried out for the antigen-binding fragment MR1 in, complex with peptide antigen. MR1 is specific for the novel fusion, junction of the mutant epidermal growth factor receptor EGFRvIII and has, been reported to have a high degree of specificity for the mutant EGFRvIII, over the wild-type EGF receptor. The structure of the complex shows that, the peptide antigen residue side-chains found by epitope mapping studies, to be critical for recognition are accommodated in pockets on the surface, of the Fv. However, the most distinctive portion of the peptide antigen, the novel fusion glycine residue, makes no contact to the Fv and does not, contribute directly to the epitope. The specificity of MR1 lies in the, ability of this glycine residue to assume the restricted conformation, needed to form a type II' beta-hairpin turn more easily, and demonstrates, that a peptide antigen can be used to generate a conformational epitope.

About this Structure

1I8I is a Protein complex structure of sequences from Mus musculus. Full crystallographic information is available from OCA.

Reference

Antibody recognition of a conformational epitope in a peptide antigen: Fv-peptide complex of an antibody fragment specific for the mutant EGF receptor, EGFRvIII., Landry RC, Klimowicz AC, Lavictoire SJ, Borisova S, Kottachchi DT, Lorimer IA, Evans SV, J Mol Biol. 2001 May 18;308(5):883-93. PMID:11352579

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