The ability to subvert E3 ubiquitin ligases with small-molecule drugs offers tremendous promise for drug discovery. A new study demonstrates how structural and computational techniques can engineer and exploit unnatural protein–protein interfaces to design selective protein degraders.
This is a preview of subscription content, access via your institution
Access options
Access Nature and 54 other Nature Portfolio journals
Get Nature+, our best-value online-access subscription
$29.99 /Â 30Â days
cancel any time
Subscribe to this journal
Receive 12 print issues and online access
$259.00 per year
only $21.58 per issue
Buy this article
- Purchase on Springer Link
- Instant access to full article PDF
Prices may be subject to local taxes which are calculated during checkout
References
Sakamoto, K. M. et al. Proc. Natl. Acad. Sci. USA 98, 8554–8559 (2001).
Nowak, R.P. et al. Nat. Chem. Biol. https://doi.org/10.1038/s41589-018-0055-y (2018).
Ito, T. et al. Science 327, 1345–1350 (2010).
Matyskiela, M. E. et al. Nature 535, 252–257 (2016).
Petzold, G., Fischer, E. S. & Thomä, N. H. Nature 532, 127–130 (2016).
Tan, X. et al. Nature 446, 640–645 (2007).
Lu, J. et al. Chem. Biol. 22, 755–763 (2015).
Winter, G. E. et al. Science 348, 1376–1381 (2015).
Gadd, M. S. et al. Nat. Chem. Biol. 13, 514–521 (2017).
Author information
Authors and Affiliations
Corresponding author
Ethics declarations
Competing interests
The author is an employee and shareholder at Celgene.
Rights and permissions
About this article
Cite this article
P. Chamberlain, P. Linkers for protein degradation. Nat Chem Biol 14, 639–640 (2018). https://doi.org/10.1038/s41589-018-0057-9
Published:
Issue Date:
DOI: https://doi.org/10.1038/s41589-018-0057-9
This article is cited by
-
Development of targeted protein degradation therapeutics
Nature Chemical Biology (2019)
