1w72

From Proteopedia

Revision as of 12:14, 30 October 2007

CRYSTAL STRUCTURE OF HLA-A1:MAGE-A1 IN COMPLEX WITH FAB-HYB3

Overview

Antibodies with T cell receptor-like specificity possess a considerable, diagnostic and therapeutic potential, but the structural basis of the, interaction between an antibody and an histocompatibility antigen has so, far not been determined. We present here the crystal structure (at 2.15 A, resolution) of the recombinant, affinity-matured human antibody fragment, Fab-Hyb3 bound to the tumor-associated human leukocyte antigen, (HLA)/peptide complex HLA-A1.MAGE-A1. Fab-Hyb3 employs a diagonal docking, mode resembling that of T cell receptors. However, other than these, natural ligands, the antibody uses only four of its six, complementarity-determining regions for direct interactions with the, target. It recognizes the C-terminal half of the MAGE-A1 peptide, the, HLA-A1 alpha1-helix, and ... [(full description)]

About this Structure

1W72 is a [Protein complex] structure of sequences from [Homo sapiens] with GOL as [ligand]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

A major histocompatibility complex-peptide-restricted antibody and t cell receptor molecules recognize their target by distinct binding modes: crystal structure of human leukocyte antigen (HLA)-A1-MAGE-A1 in complex with FAB-HYB3., Hulsmeyer M, Chames P, Hillig RC, Stanfield RL, Held G, Coulie PG, Alings C, Wille G, Saenger W, Uchanska-Ziegler B, Hoogenboom HR, Ziegler A, J Biol Chem. 2005 Jan 28;280(4):2972-80. Epub 2004 Nov 10. PMID:15537658

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