Recent progress with FKBP-derived destabilizing domains

Bioorg Med Chem Lett. 2008 Nov 15;18(22):5941-4. doi: 10.1016/j.bmcl.2008.09.043. Epub 2008 Sep 12.

Abstract

The FKBP-derived destabilizing domains are increasingly being used to confer small molecule-dependent stability to many different proteins. The L106P domain confers instability to yellow fluorescent protein when it is fused to the N-terminus, the C-terminus, or spliced into the middle of yellow fluorescent protein, however multiple copies of L106P do not confer greater instability. These engineered destabilizing domains are not dominant to endogenous degrons that regulate protein stability.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Amino Acid Motifs
  • Cell Cycle / drug effects
  • Cyclin B / metabolism
  • Cyclin B1
  • HeLa Cells
  • Humans
  • Models, Molecular*
  • Structure-Activity Relationship
  • Tacrolimus Binding Proteins / chemistry*
  • Tacrolimus Binding Proteins / genetics
  • Tacrolimus Binding Proteins / metabolism

Substances

  • CCNB1 protein, human
  • Cyclin B
  • Cyclin B1
  • Tacrolimus Binding Proteins