Using nuclear magnetic resonance technology, researchers led by Gerhard Wagner, the Elkan Blout professor of biological chemistry and molecular pharmacology, have determined its atomic structure. Current apoptosis research tries to understand how the mitochondria sustain damage after death-inducing signals have penetrated the cell. BID is a major suspect.
Mitochondrial damage can seal the cell's fate by activating caspases, the death enzymes.
Bcl-x L more readily. BID has another trick up its sleeve, the scientists report. Its structure resembles that of bacterial toxins that bore holes in cell membranes, suggesting it might insert itself into the mitochondrial membrane and disturb its electric balance. The latest in a series of studies revealing the structures of cell death molecules, this work broadens a perplexing observation in the field. Cell death proteins that are only distantly related by sequence closely resemble each other in structure yet can have opposing ultimate effects in the cell.