JavaScript is disabled for your browser. Some features of this site may not work without it.
Structure of Bcl-xL-Bak peptide complex : recognition between regulators of Apoptosis.
| 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. |
Files in this item
| Files | Size | Format | View |
|---|---|---|---|
|
There are no files associated with this item. |
|||
|
|
- Get published version (via Digital Object Identifier) |
This item appears in the following Collection(s)
Statistics
Total views
| All Items | Views |
| Structure of Bcl-xL-Bak peptide complex : recognition between regulators of Apoptosis. | 235 |
