1FAD

DEATH DOMAIN OF FAS-ASSOCIATED DEATH DOMAIN PROTEIN, RESIDUES 89-183

Summary for 1FAD

• Entry DOI: 10.2210/pdb1fad/pdb
• Descriptor: PROTEIN (FADD PROTEIN) (1 entity in total)
• Functional Keywords: apoptosis, fadd, death domain
• Biological source: Mus musculus (house mouse)
• Total number of polymer chains: 1
• Total formula weight: 11088.69

Authors

Jeong, E.-J.,Bang, S.,Lee, T.H.,Park, Y.-I.,Sim, W.-S.,Kim, K.-S. (deposition date: 1999-03-23, release date: 1999-07-06, Last modification date: 2023-12-27)

Primary citation

Jeong, E.J.,Bang, S.,Lee, T.H.,Park, Y.I.,Sim, W.S.,Kim, K.S.
The solution structure of FADD death domain. Structural basis of death domain interactions of Fas and FADD.
J.Biol.Chem., 274:16337-16342, 1999

PubMed Abstract: A signal of Fas-mediated apoptosis is transferred through an adaptor protein Fas-associated death domain protein (FADD) by interactions between the death domains of Fas and FADD. To understand the signal transduction mechanism of Fas-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 Fas and FADD analyzed by site-directed mutagenesis indicate that charged residues in helices alpha2 and alpha3 are involved in death domain interactions, and the interacting helices appear to interact in anti-parallel pattern, alpha2 of FADD with alpha3 of Fas and vice versa.

PubMed: 10347191
DOI: 10.1074/jbc.274.23.16337

Experimental method

SOLUTION NMR