Recent progress with FKBP-derived destabilizing domains

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

Research output: Contribution to journalArticle

26 Citations (Scopus)

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

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Tacrolimus Binding Proteins
Proteins
Protein Stability
Molecules

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

Cite this

Recent progress with FKBP-derived destabilizing domains. / Chu, Bernard W.; Banaszynski, Laura A.; Chen, Ling chun; Wandless, Thomas J.

In: Bioorganic and Medicinal Chemistry Letters, Vol. 18, No. 22, 15.11.2008, p. 5941-5944.

Research output: Contribution to journalArticle

Chu, Bernard W. ; Banaszynski, Laura A. ; Chen, Ling chun ; Wandless, Thomas J. / Recent progress with FKBP-derived destabilizing domains. In: Bioorganic and Medicinal Chemistry Letters. 2008 ; Vol. 18, No. 22. pp. 5941-5944.
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