Recent progress with FKBP-derived destabilizing domains

Bernard W. Chu, Laura A. Banaszynski, Ling chun Chen, Thomas J. Wandless

Research output: Contribution to journalArticlepeer-review

29 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)5941-5944
Number of pages4
JournalBioorganic and Medicinal Chemistry Letters
Volume18
Issue number22
DOIs
StatePublished - Nov 15 2008

Keywords

  • Cell cycle
  • Cyclin
  • Destabilizing domain
  • Proteasome
  • Protein degradation
  • Shield-1

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Medicine
  • Molecular Biology
  • Pharmaceutical Science
  • Drug Discovery
  • Clinical Biochemistry
  • Organic Chemistry

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