Structure of Bcl-xL-Bak peptide complex: recognition between regulators of apoptosis.
Science
; 275(5302): 983-6, 1997 Feb 14.
Article
en En
| MEDLINE
| ID: mdl-9020082
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.
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Bases de datos:
MEDLINE
Asunto principal:
Conformación Proteica
/
Proteínas Proto-Oncogénicas
/
Proteínas Proto-Oncogénicas c-bcl-2
/
Proteínas de la Membrana
Idioma:
En
Revista:
Science
Año:
1997
Tipo del documento:
Article
País de afiliación:
Estados Unidos