title: Structural Characterizations of the Fas Receptor and the Fas-Associated Protein with Death Domain Interactions.
abstract: The Fas receptor is a representative death receptor, and the Fas-associated protein with death domain (FADD) is a crucial adapter protein needed to support the Fas receptor's activity. The Fas-FADD interactions constitute an important signaling pathway that ultimately induces apoptosis or programmed cell death in biological systems. The interactions responsible for this cell-death process are governed by the binding process of the Fas ligand to the Fas, followed by the caspase cascade activation. Using a computational approach, the present communication explores certain essential structural aspects of the Fas-FADD death domains and their interfacial interactions.
authors.affiliation: Department of Chemistry and Biomolecular Science, and Center for Advanced Materials Processing, Clarkson University, 8 Clarkson Avenue, Potsdam, NY, 13699-5665, USA. urmi@clarkson.edu.
authors.forename: Urmi
authors.initials: U
authors.lastname: Roy
mesh_terms: D053200:Fas-Associated Death Domain Protein / Q000737:chemistry* / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy; D056004:Molecular Dynamics Simulation; D011485:Protein Binding; D019014:fas Receptor / Q000737:chemistry* / Q000378:metabolism*
chemical_list: D053200:Fas-Associated Death Domain Protein; D019014:fas Receptor
keywords: Death domain; Fas; Fas-associated protein with death domain; Immunology; Structural biology