A Conserved Allosteric Pathway in Tyrosine Kinase Regulation

William M. Marsiglia, Joseph Katigbak, Sijin Zheng, Moosa Mohammadi, Yingkai Zhang, Nathaniel J. Traaseth

Research output: Contribution to journalArticlepeer-review


Marsiglia et al. reveal that the kinase molecular brake is coupled to the DFG motif through an allosteric pathway involving an isoleucine residue that locks the phenylalanine of the DFG motif activation loop in an inactive conformation. Pathogenic mutations that target the molecular brake activate the enzyme by perturbing this allosteric network.

Original languageEnglish (US)
Pages (from-to)1308-1315.e3
Issue number8
StatePublished - Aug 6 2019


  • FGF receptor
  • NMR spectroscopy
  • allostery
  • pathogenic mutations
  • tyrosine kinases

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology


Dive into the research topics of 'A Conserved Allosteric Pathway in Tyrosine Kinase Regulation'. Together they form a unique fingerprint.

Cite this