Structure of Bcl-xL-Bak Peptide Complex: Recognition Between Regulators of Apoptosis
M Sattler, H Liang, D Nettesheim, RP Meadows… - Science, 1997 - science.org
Science, 1997•science.org
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 …
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 …
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.
AAAS