Structural highlights
Function
[BID_HUMAN] The major proteolytic product p15 BID allows the release of cytochrome c (By similarity). Isoform 1, isoform 2 and isoform 4 induce ICE-like proteases and apoptosis. Isoform 3 does not induce apoptosis. Counters the protective effect of Bcl-2.[1]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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 alpha helices where two central hydrophobic helices are surrounded by six amphipathic ones. The fold resembles poreforming bacterial toxins and shows similarity to BCL-XL although sequence homology to BCL-XL is limited to the 16-residue BH3 domain. Furthermore, we modeled a complex of BCL-XL and BID by aligning the BID and BAK BH3 motifs in the known BCL-XL-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.
Solution structure of BID, an intracellular amplifier of apoptotic signaling.,Chou JJ, Li H, Salvesen GS, Yuan J, Wagner G Cell. 1999 Mar 5;96(5):615-24. PMID:10089877[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Renshaw SA, Dempsey CE, Barnes FA, Bagstaff SM, Dower SK, Bingle CD, Whyte MK. Three novel Bid proteins generated by alternative splicing of the human Bid gene. J Biol Chem. 2004 Jan 23;279(4):2846-55. Epub 2003 Oct 28. PMID:14583606 doi:http://dx.doi.org/10.1074/jbc.M309769200
- ↑ Chou JJ, Li H, Salvesen GS, Yuan J, Wagner G. Solution structure of BID, an intracellular amplifier of apoptotic signaling. Cell. 1999 Mar 5;96(5):615-24. PMID:10089877
