Jeong, EJ Bang, S Lee, TH Park, YI Sim, WS Kim, KS 2024-01-21T15:32:13Z 2024-01-21T15:32:13Z 2021-09-05 1999-06 0021-9258 https://pubs.kist.re.kr/handle/201004/142165 A signal of Pas-mediated apoptosis is transferred through an adaptor protein Pas-associated death domain protein (FADD) by interactions between the death domains of Pas and FADD. To understand the signal transduction mechanism of Pas-mediated apoptosis, we solved the solution structure of a murine FADD death domain. It consists of six helices arranged in a similar fold to the other death domains. The interactions between the death domains of Pas and FADD analyzed by site-directed mutagenesis indicate that charged residues in helices alpha 2 and alpha 3 are involved in death domain interactions, and the interacting helices appear to interact in anti-parallel pattern, alpha 2 of FADD with alpha 3 of Fas and vice versa. English AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC The solution structure of FADD death domain - Structural basis of death domain interactions of Fas and FADD Article 10.1074/jbc.274.23.16337 1 JOURNAL OF BIOLOGICAL CHEMISTRY, v.274, no.23, pp.16337 - 16342 JOURNAL OF BIOLOGICAL CHEMISTRY 274 23 16337 16342 N scie scopus 000080668600051 2-s2.0-0033522889 Biochemistry & Molecular Biology Biochemistry & Molecular Biology Article PROTEIN-STRUCTURE DETERMINATION SIGNALING COMPLEX DISC NMR STRUCTURE INDUCED APOPTOSIS DIRECT REFINEMENT RECEPTOR SIGNALS EFFECTOR DOMAIN CD95 FAS/APO-1 CELL-DEATH RESONANCE FADD death domain