Triggering Cell Death
- 1 October 1999
- journal article
- Published by Elsevier BV in Molecular Cell
- Vol. 4 (4), 563-571
- https://doi.org/10.1016/s1097-2765(00)80207-5
Abstract
Formation of a complex between Apo2L (also called TRAIL) and its signaling receptors, DR4 and DR5, triggers apoptosis by inducing the oligomerization of intracellular death domains. We report the crystal structure of the complex between Apo2L and the ectodomain of DR5. The structure shows three elongated receptors snuggled into long crevices between pairs of monomers of the homotrimeric ligand. The interface is divided into two distinct patches, one near the bottom of the complex close to the receptor cell surface and one near the top. Both patches contain residues that are critical for high-affinity binding. A comparison to the structure of the lymphotoxin-receptor complex suggests general principles of binding and specificity for ligand recognition in the TNF receptor superfamily.Keywords
This publication has 41 references indexed in Scilit:
- Safety and antitumor activity of recombinant soluble Apo2 ligandJCI Insight, 1999
- Apoptosis by Death FactorCell, 1997
- Programmed Cell Death in Animal DevelopmentCell, 1997
- [20] Processing of X-ray diffraction data collected in oscillation modeMethods in Enzymology, 1997
- Induction of Apoptosis by Apo-2 Ligand, a New Member of the Tumor Necrosis Factor Cytokine FamilyJournal of Biological Chemistry, 1996
- The CCP4 suite: programs for protein crystallographyActa Crystallographica Section D-Biological Crystallography, 1994
- A novel domain within the 55 kd TNF receptor signals cell deathCell, 1993
- Emerging families of cytokines and receptorsCurrent Biology, 1993
- Free R value: a novel statistical quantity for assessing the accuracy of crystal structuresNature, 1992
- Aspartic acid 50 and tyrosine 108 are essential for receptor binding and cytotoxic activity of tumour necrosis factor beta (lymphotoxin)Protein Engineering, Design and Selection, 1991