Structure of Bcl-x L -Bak Peptide Complex: Recognition Between Regulators of Apoptosis
- 14 February 1997
- journal article
- other
- Published by American Association for the Advancement of Science (AAAS) in Science
- Vol. 275 (5302) , 983-986
- https://doi.org/10.1126/science.275.5302.983
Abstract
Heterodimerization between members of the Bcl-2 family of proteins is a key event in the regulation of programmed cell death. The molecular basis for heterodimer formation was investigated by determination of the solution structure of a complex between the survival protein Bcl-xL and the death-promoting region of the Bcl-2-related protein Bak. The structure and binding affinities of mutant Bak peptides indicate that the Bak peptide adopts an amphipathic α helix that interacts with Bcl-xL through hydrophobic and electrostatic interactions. Mutations in full-length Bak that disrupt either type of interaction inhibit the ability of Bak to heterodimerize with Bcl-xL.Keywords
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