Conversion of Bim-BH3 from Activator to Inhibitor of Bak through Structure-Based Design

Jason M. Brouwer, Ping Lan, Angus D. Cowan, Jonathan P. Bernardini, Richard W. Birkinshaw, Mark F. van Delft, Brad E. Sleebs, Adeline Y. Robin, Ahmad Wardak, Iris K. Tan, Boris Reljic, Erinna F. Lee, W. Douglas Fairlie, Melissa J. Call, Brian J. Smith, Grant Dewson, Guillaume Lessene, Peter M. Colman, Peter E. Czabotar

Research output: Contribution to journalArticlepeer-review

54 Citations (Scopus)

Abstract

Certain BH3-only proteins transiently bind and activate Bak and Bax, initiating their oligomerization and the permeabilization of the mitochondrial outer membrane, a pivotal step in the mitochondrial pathway to apoptosis. Here we describe the first crystal structures of an activator BH3 peptide bound to Bak and illustrate their use in the design of BH3 derivatives capable of inhibiting human Bak on mitochondria. These BH3 derivatives compete for the activation site at the canonical groove, are the first engineered inhibitors of Bak activation, and support the role of key conformational transitions associated with Bak activation. Brouwer et al. describe the first crystal structures of BH3-only peptides bound to Bak, which reveal a cavity that may be important for activation. They then use structure-based design to alter the Bim-BH3 peptide and convert it from an activator to an inhibitor of Bak.

Original languageEnglish
Pages (from-to)659-672.e9
Number of pages24
JournalMolecular Cell
Volume68
Issue number4
DOIs
Publication statusPublished - 16 Nov 2017

Keywords

  • apoptosis
  • Bak
  • Bcl-2 family
  • Bim
  • inhibitor
  • non-natural amino acid

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

Fingerprint

Dive into the research topics of 'Conversion of Bim-BH3 from Activator to Inhibitor of Bak through Structure-Based Design'. Together they form a unique fingerprint.

Cite this