2BID

HUMAN PRO-APOPTOTIC PROTEIN BID

Summary for 2BID

• Entry DOI: 10.2210/pdb2bid/pdb
• NMR Information: BMRB: 5340
• Descriptor: PROTEIN (BID) (1 entity in total)
• Functional Keywords: programmed cell death, apoptosis regulation and amplification, apoptosis
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm (By similarity). BH3-interacting domain death agonist p15: Mitochondrion membrane (By similarity). BH3-interacting domain death agonist p13: Mitochondrion membrane (By similarity). Isoform 1: Cytoplasm. Isoform 3: Cytoplasm. Isoform 2: Mitochondrion membrane: P55957
• Total number of polymer chains: 1
• Total formula weight: 22165.83

Authors

Chou, J.J.,Li, H.,Salvesen, G.S.,Yuan, J.,Wagner, G. (deposition date: 1999-01-27, release date: 2000-02-02, Last modification date: 2023-12-27)

Primary citation

Chou, J.J.,Li, H.,Salvesen, G.S.,Yuan, J.,Wagner, G.
Solution structure of BID, an intracellular amplifier of apoptotic signaling.
Cell(Cambridge,Mass.), 96:615-624, 1999

PubMed Abstract: 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.

PubMed: 10089877
DOI: 10.1016/S0092-8674(00)80572-3

Experimental method

SOLUTION NMR