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Fesik Lab

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

AUTHORS

Sattler M , Liang H , Nettesheim D , Meadows RP , Harlan JE , Eberstadt M , Yoon HS , Shuker SB , Chang BS , Minn AJ , Thompson CB , Fesik SW . Science. 1997 2 14; 275(5302). 983-986

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.