The structure of the full-length tetrameric PKA regulatory RIIβ complex reveals the mechanism of allosteric PKA activation

  • Elkins J
  • Knapp S
  • 15

    Readers

    Mendeley users who have this article in their library.
  • 1

    Citations

    Citations of this article.

Abstract

The catalytic activity of protein kinases is usually tightly controlled by posttranslational modifications and diverse sets of regulatory proteins. Protein kinases are highly dynamic enzymes, and structures of kinases in various activation states and costructures with regulatory proteins have provided critical insights into the complex regulatory mechanisms of this large and diverse protein family. The crystal structure of protein kinase A (PKA) provided a reference model for our understanding of kinase catalytic function. Now, more than two decades later, the high-resolution model of a full-length tetrameric PKA holoenzyme has been published, revealing the structural mechanisms underlying allosteric PKA activation.

Get free article suggestions today

Mendeley saves you time finding and organizing research

Sign up here
Already have an account ?Sign in

Find this document

Authors

Cite this document

Choose a citation style from the tabs below

Save time finding and organizing research with Mendeley

Sign up for free