Structure of Bcl-x <sub>L</sub> -Bak Peptide Complex: Recognition Between Regulators of Apoptosis
Michael Sattler(Discovery Laboratories (United States)), Heng Liang(Discovery Laboratories (United States)), David G. Nettesheim(Discovery Laboratories (United States)), Robert Meadows(Discovery Laboratories (United States)), John E. Harlan(Discovery Laboratories (United States)), Matthias Eberstadt(Discovery Laboratories (United States)), Ho Sup Yoon(Discovery Laboratories (United States)), Suzanne B. Shuker(Discovery Laboratories (United States)), Brian S. Chang(Howard Hughes Medical Institute), Andy J. Minn(Howard Hughes Medical Institute), Craig B. Thompson(Howard Hughes Medical Institute), Stephen W. Fesik(Discovery Laboratories (United States))
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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 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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