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 Cited by 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: 10089877DOI: 10.1016/S0092-8674(00)80572-3 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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