Molecular dynamics simulations reveal the conformational dynamics of Arabidopsis thaliana BRI1 and BAK1 receptor-like kinases

Alexander S. Moffett, Kyle W. Bender, Steven C. Huber, Diwakar Shukla

Research output: Contribution to journalArticlepeer-review

Abstract

The structural motifs responsible for activation and regulation of eukaryotic protein kinases in animals have been studied extensively in recent years, and a coherent picture of their activation mechanisms has begun to emerge. In contrast, non-animal eukaryotic protein kinases are not as well understood from a structural perspective, representing a large knowledge gap. To this end, we investigated the conformational dynamics of two key Arabidopsis thaliana receptor-like kinases, brassinosteroid-insensitive 1 (BRI1) and BRI1-associated kinase 1 (BAK1), through extensive molecular dynamics simulations of their fully phosphorylated kinase domains. Molecular dynamics simulations calculate the motion of each atom in a protein based on classical approximations of interatomic forces, giving researchers insight into protein function at unparalleled spatial and temporal resolutions. We found that in an otherwise “active” BAK1 the C helix is highly disordered, a hallmark of deactivation, whereas the BRI1 C helix is moderately disordered and displays swinging behavior similar to numerous animal kinases. An analysis of all known sequences in the A. thaliana kinome found that C helix disorder may be a common feature of plant kinases.

Original languageEnglish (US)
Pages (from-to)12643-12652
Number of pages10
JournalJournal of Biological Chemistry
Volume292
Issue number30
DOIs
StatePublished - Jul 21 2017

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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