Allosteric Activation of PI3Kα Results in Dynamic Access to Catalytically Competent Conformations

Mayukh Chakrabarti, Sandra B Gabelli, L. Mario Amzel

Research output: Contribution to journalArticlepeer-review

Abstract

PI3Kα is a phospholipid kinase that phosphorylates PIP2 to generate PIP3, a scaffold for many important downstream signaling pathways. In this paper, Chakrabarti et al. demonstrate that dynamic allostery can increase the population of PI3Kα states compatible with catalysis, which has implications for the development of new PI3K therapeutics.

Original languageEnglish (US)
Pages (from-to)465-474.e5
JournalStructure
Volume28
Issue number4
DOIs
StatePublished - Apr 7 2020

Keywords

  • catalytic mechanism
  • dynamic allostery
  • enzyme activation
  • molecular dynamics
  • phosphoinositide (3,4,5)-trisphosphate
  • phosphoinositide (4,5)-bisphosphate
  • phosphoinositide kinase
  • population increase
  • signaling pathway

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

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