title: Structural studies of death receptors.
abstract: This chapter describes reports of the structural characterization of death ligands and death receptors (DRs) from the tumor necrosis factor (TNF) and TNF receptor families. The review discusses the interactions of these proteins with agonist ligands, inhibitors, and downstream signaling molecules. Though historically labeled as being implicated in programmed cell death, the function of these proteins extends to nonapoptotic pathways. The review highlights, from a structural biology perspective, the complexity of DR signaling and the ongoing challenge to discern the precise mechanisms that occur at the point of DR activation, including how the degree to which the receptors are induced to cluster may be related to the nature of the impact upon the cell. The potential for posttranslational modification and receptor internalization to play roles in DR signaling is briefly discussed.
authors: Division of Molecular Structure, Medical Research Council, National Institute for Medical Research, London, United Kingdom. Electronic address: pdrisco@nimr.mrc.ac.uk.
authors: Paul C
authors: PC
authors: Driscoll
mesh_terms: D017209:Apoptosis / Q000235:genetics*; D018360:Crystallography, X-Ray; D006801:Humans; D008024:Ligands; D009682:Magnetic Resonance Spectroscopy; D011487:Protein Conformation; D011499:Protein Processing, Post-Translational / Q000235:genetics; D053218:Receptors, Death Domain / Q000737:chemistry* / Q000378:metabolism; D015398:Signal Transduction; D014409:Tumor Necrosis Factor-alpha / Q000737:chemistry*
chemical_list: D008024:Ligands; D053218:Receptors, Death Domain; D014409:Tumor Necrosis Factor-alpha
keywords: Death domain; Death receptor; Death-inducing signaling complex; NMR spectroscopy; Tumor necrosis factor; X-ray crystallography