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- Title
Structure of Bcl-xL-Bak peptide complex: recognition between regulators of apoptosis.
- Authors
Sattler, M; Liang, H; Nettesheim, D; Meadows, R P; Harlan, J E; Eberstadt, M; Yoon, H S; Shuker, S B; Chang, B S; Minn, A J; Thompson, C B; Fesik, S W
- 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.
- Publication
Science (New York, N.Y.), 1997, Vol 275, Issue 5302, p983
- ISSN
0036-8075
- Publication type
Journal Article
- DOI
10.1126/science.275.5302.983