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Structure of Bcl-xL-Bak Peptide Complex: Recognition Between Regulators of Apoptosis

Science  14 Feb 1997:
Vol. 275, Issue 5302, pp. 983-986
DOI: 10.1126/science.275.5302.983

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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.

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