-
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.
Pharmaceutical Discovery Division, Abbott Laboratories, Abbott Park, IL 60064, USA.
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.
PMID: 9020082 [PubMed - indexed for MEDLINE]
-
Cited by over 100 PubMed Central articles
-
Small-molecule Bcl-2 antagonists as targeted therapy in oncology.
Warr MR, Shore GC.
Curr Oncol. 2008 Dec; 15(6):256-61.
[Curr Oncol. 2008]
-
Apoptosis is triggered when prosurvival Bcl-2 proteins cannot restrain Bax.
Fletcher JI, Meusburger S, Hawkins CJ, Riglar DT, Lee EF, Fairlie WD, Huang DC, Adams JM.
Proc Natl Acad Sci U S A. 2008 Nov 25; 105(47):18081-7. Epub 2008 Nov 3.
[Proc Natl Acad Sci U S A. 2008]
-
BAX activation is initiated at a novel interaction site.
Gavathiotis E, Suzuki M, Davis ML, Pitter K, Bird GH, Katz SG, Tu HC, Kim H, Cheng EH, Tjandra N, et al.
Nature. 2008 Oct 23; 455(7216):1076-81.
[Nature. 2008]
- » See all...
Structures reported by this article