2bid
HUMAN PRO-APOPTOTIC PROTEIN BID
OverviewOverview
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.
About this StructureAbout this Structure
2BID is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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 Page seeded by OCA on Sat May 3 20:19:50 2008