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. 1997 Feb 14;275(5302):983-6.
doi: 10.1126/science.275.5302.983.

Structure of Bcl-xL-Bak peptide complex: recognition between regulators of apoptosis

M Sattler  1 , H Liang, D Nettesheim, R P Meadows, J E Harlan, M Eberstadt, H S Yoon, S B Shuker, B S Chang, A J Minn, C B Thompson, S W Fesik
Affiliations

Structure of Bcl-xL-Bak peptide complex: recognition between regulators of apoptosis

M Sattler et al. Science. .

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 alpha 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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