The solution structure of FADD death domain. Structural basis of death domain interactions of Fas and FADD

Eui Jun Jeong, Sook Hee Bang, Tae Ho Lee, Young In Park, Woong Seop Sim, Key Sun Kim

Research output: Contribution to journalArticle

96 Citations (Scopus)

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 α2 and α3 are involved in death domain interactions, and the interacting helices appear to interact in anti-parallel pattern, α2 of FADD with α3 of Fas and vice versa.

Original languageEnglish
Pages (from-to)16337-16342
Number of pages6
JournalJournal of Biological Chemistry
Volume274
Issue number23
DOIs
Publication statusPublished - 1999 Jun 4

Fingerprint

Fas-Associated Death Domain Protein
Apoptosis
Signal transduction
Mutagenesis
Site-Directed Mutagenesis
Signal Transduction
Death Domain
Protein Domains
Proteins

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Jeong, Eui Jun ; Bang, Sook Hee ; Lee, Tae Ho ; Park, Young In ; Sim, Woong Seop ; Kim, Key Sun. / The solution structure of FADD death domain. Structural basis of death domain interactions of Fas and FADD. In: Journal of Biological Chemistry. 1999 ; Vol. 274, No. 23. pp. 16337-16342.
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The solution structure of FADD death domain. Structural basis of death domain interactions of Fas and FADD. / Jeong, Eui Jun; Bang, Sook Hee; Lee, Tae Ho; Park, Young In; Sim, Woong Seop; Kim, Key Sun.

In: Journal of Biological Chemistry, Vol. 274, No. 23, 04.06.1999, p. 16337-16342.

Research output: Contribution to journalArticle

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AU - Bang, Sook Hee

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AU - Kim, Key Sun

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AB - 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 α2 and α3 are involved in death domain interactions, and the interacting helices appear to interact in anti-parallel pattern, α2 of FADD with α3 of Fas and vice versa.

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