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

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

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Title: Structure of Bcl-xL-Bak peptide complex : recognition between regulators of Apoptosis.
Author: Sattler, Michael.; Liang, Heng.; Nettesheim, David G.; Meadows, Robert P.; Harlan, John E.; Eberstadt, Matthias.; Yoon, Ho Sup.; Shuker, Suzanne B.; Chang, Brian S.; Minn, Andy J.; Thompson, Craig B.; Fesik, Stephen W.
Copyright year: 1997
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 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.
Subject: DRNTU::Business::Public relations::Crisis communication.
Type: Journal Article
Series/ Journal Title: Science
School: School of Biological Sciences
Rights: © 1997 American Association for the Advancement of Science.

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