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

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 275 (5302): 983-6

PMID: 9020082 · DOI:10.1126/science.275.5302.983

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.

MeSH Terms (15)

Amino Acid Sequence Apoptosis bcl-2 Homologous Antagonist-Killer Protein bcl-X Protein Crystallography, X-Ray Dimerization Magnetic Resonance Spectroscopy Membrane Proteins Models, Molecular Molecular Sequence Data Protein Conformation Protein Structure, Secondary Proto-Oncogene Proteins Proto-Oncogene Proteins c-bcl-2 Sequence Deletion

Connections (1)

This publication is referenced by other Labnodes entities: