Triggering Cell Death
Copyright policy )Triggering Cell Death
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.
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Models, Molecular, Membrane Glycoproteins, Tumor Necrosis Factor-alpha, Molecular Sequence Data, Molecular Conformation, Apoptosis, Cell Biology, Crystallography, X-Ray, Peptide Fragments, Protein Structure, Secondary, Receptors, Tumor Necrosis Factor, Recombinant Proteins, Cell Line, TNF-Related Apoptosis-Inducing Ligand, Receptors, TNF-Related Apoptosis-Inducing Ligand, Escherichia coli, Amino Acid Sequence, Apoptosis Regulatory Proteins, Molecular Biology, Lymphotoxin-alpha, Sequence Alignment, Protein Binding
Models, Molecular, Membrane Glycoproteins, Tumor Necrosis Factor-alpha, Molecular Sequence Data, Molecular Conformation, Apoptosis, Cell Biology, Crystallography, X-Ray, Peptide Fragments, Protein Structure, Secondary, Receptors, Tumor Necrosis Factor, Recombinant Proteins, Cell Line, TNF-Related Apoptosis-Inducing Ligand, Receptors, TNF-Related Apoptosis-Inducing Ligand, Escherichia coli, Amino Acid Sequence, Apoptosis Regulatory Proteins, Molecular Biology, Lymphotoxin-alpha, Sequence Alignment, Protein Binding
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