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Selective inhibition of STAT3 signaling using monobodies targeting the coiled-coil and N-terminal domains

Authors
  • La Sala, Grégory1
  • Michiels, Camille2
  • Kükenshöner, Tim1
  • Brandstoetter, Tania3
  • Maurer, Barbara3
  • Koide, Akiko4, 5
  • Lau, Kelvin6
  • Pojer, Florence6
  • Koide, Shohei5, 4
  • Sexl, Veronika3
  • Dumoutier, Laure2
  • Hantschel, Oliver1, 7
  • 1 Swiss Institute for Experimental Cancer Research (ISREC), School of Life Sciences, École polytechnique fédérale de Lausanne (EPFL), Station 19, Lausanne, 1015, Switzerland , Lausanne (Switzerland)
  • 2 Université catholique de Louvain, Brussels, 1200, Belgium , Brussels (Belgium)
  • 3 University of Veterinary Medicine, Vienna, Austria , Vienna (Austria)
  • 4 New York University School of Medicine, 522 1st Avenue, New York, NY, 10016, USA , New York (United States)
  • 5 New York University Langone Health, 522 1st Avenue, New York, NY, 10016, USA , New York (United States)
  • 6 Protein Crystallography Core Facility, School of Life Sciences, École polytechnique fédérale de Lausanne, Station 19, Lausanne, 1015, Switzerland , Lausanne (Switzerland)
  • 7 Philipps-University of Marburg, Karl-von-Frisch-Straße 1, Marburg, 35032, Germany , Marburg (Germany)
Type
Published Article
Journal
Nature Communications
Publisher
Springer Nature
Publication Date
Aug 17, 2020
Volume
11
Issue
1
Identifiers
DOI: 10.1038/s41467-020-17920-z
Source
Springer Nature
License
Green

Abstract

STAT3 is an attractive therapeutic target but its homology with other STAT proteins complicates the development of selective inhibitors. Here, the authors develop monobodies with high affinity and selectivity for STAT3 and show that they can interfere with cellular STAT3 activity.

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