Solution Structure for BID, and Intracellular Amplifier of Apoptotic Signaling

an intracellular amplifier of apoptotic signaling

Solution structure of BID, an intracellular amplifier of apoptotic signaling.

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.

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.

We report here that BID, a BH3 domain-containing proapoptotic Bcl2 family
member, is a specific proximal substrate of Casp8 in the Fas apoptotic
signaling pathway. While full-length BID is localized in cytosol, truncated BID
(tBID) translocates to mitochondria and thus transduces apoptotic signals from
cytoplasmic membrane to mitochondria. tBID induces first the clustering of
mitochondria around the nuclei and release of cytochrome c independent of
caspase activity, and then the loss of mitochondrial membrane potential, cell
shrinkage, and nuclear condensation in a caspase-dependent fashion.
Coexpression of BclxL inhibits all the apoptotic changes induced by tBID. Our
results indicate that BID is a mediator of mitochondrial damage induced by
Casp8.

Li H, Zhu H, Xu CJ, Yuan J.
Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis.
Cell. 1998 Aug 21;94(4):491-501.

Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis.

The protein was overexpressed as a GST-fusion protein.
So there are additional two N-terminal residues GS.

Nmr Structures Of Human Apoptotic Protein Tbid In Lppg Micelle

BH3-interacting domain death agonist [synthetic construct]

BH3 interacting domain death agonist [Homo sapiens]

BH3-interacting domain death agonist [Pongo abelii]

BH3-interacting domain death agonist isoform 2 [Homo sapiens]

BH3-interacting domain death agonist isoform 3 [Homo sapiens]

RecName: Full=BH3-interacting domain death agonist; AltName: Full=p22 BID; Short=BID; Contains: RecName: Full=BH3-interacting d