1dg6

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spinqualitylabelsall models 1dg6, resolution 1.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

CRYSTAL STRUCTURE OF APO2L/TRAIL

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

Apoptosis-inducing ligand 2 (Apo2L, also called TRAIL), a member of the, tumor necrosis factor (TNF) family, induces apoptosis in a variety of, human tumor cell lines but not in normal cells [Wiley, S. R., Schooley, K., Smolak, P. J., Din, W. S., Huang, C.-P., Nicholl, J. K., Sutherland, G. R., Smith, T. D., Rauch, C., Smith, C. A., and Goodwin, R. G. (1995), Immunity 3, 673-682; Pitti, R. M., Marsters, S. A., Ruppert, S., Donahue, C. J., Moore, A., and Ashkenazi, A. (1996) J. Biol. Chem. 271, 12687-12690]. Here we describe the structure of Apo2L at 1.3 A resolution, and use alanine-scanning mutagenesis to map the receptor contact regions., The structure reveals a homotrimeric protein that resembles TNF with, receptor-binding epitopes at the interface between monomers. A zinc ion is, buried at the trimer interface, coordinated by the single cysteine residue, of each monomer. The zinc ion is required for maintaining the native, structure and stability and, hence, the biological activity of Apo2L. This, is the first example of metal-dependent oligomerization and function of a, cytokine.

Disease

Known disease associated with this structure: Squamous cell carcinoma, head and neck OMIM:[603612]

About this Structure

1DG6 is a Single protein structure of sequence from Homo sapiens with ZN and CL as ligands. Full crystallographic information is available from OCA.

Reference

A unique zinc-binding site revealed by a high-resolution X-ray structure of homotrimeric Apo2L/TRAIL., Hymowitz SG, O'Connell MP, Ultsch MH, Hurst A, Totpal K, Ashkenazi A, de Vos AM, Kelley RF, Biochemistry. 2000 Feb 1;39(4):633-40. PMID:10651627

Page seeded by OCA on Mon Nov 12 16:32:05 2007