Solution structure of BID, an intracellular amplifier of apoptotic signaling

James J. Chou, Honglin Li, Guy S. Salvesen, Junying Yuan, Gerhard Wagner

Research output: Contribution to journalArticlepeer-review

423 Scopus citations


We report the solution structure of BID, an intracellular cross-talk agent that can amplify FAS/TNF apoptotic signal through the mitochondria death pathway after Caspase 8 cleavage. BID contains eight α helices where two central hydrophobic helices a re surrounded by six amphipathic ones. The fold resembles pore-forming bacterial toxins and shows similarity to BCLX(L) although sequence homology to BCL-X(L) is limited to the 16-residue BH3 domain. Furthermore, we modeled a complex of BCL-X, and BID by aligning the BID and BAK BH3 motifs in the known BCL-X(L)-BAK BH3 complex. Additionally, we show that the overall structure of BID is preserved after cleavage by Caspase 8. We propose that BID has both BH3 domain-dependent and -independent modes of action in inducing mitochondrial damage.

Original languageEnglish (US)
Pages (from-to)615-624
Number of pages10
Issue number5
StatePublished - Mar 5 1999
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry, Genetics and Molecular Biology(all)


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