Confirming the Importance of the R-Spine: New Insights into Protein Kinase Regulation

Richard Robinson

doi:10.1371/journal.pbio.1001681

Abstract

Confirming the Importance of the R-Spine: New Insights into Protein Kinase Regulation

Highlights

Phosphorylation is a ubiquitous means of changing a protein’s behavior
The requirements of rational drug design, as well as pure human curiosity, have led researchers to try to understand the structural features of protein kinases that contribute to their regulation. In this issue of PLOS Biology, Hiruy Meharena, Alexandr Kornev, and colleagues demonstrate the central importance of one structural element common to all protein kinases, and identify key amino acids that contribute to the stability of the catalytic core
The unusual characteristic of the catalytic spine (C-spine) is that the adenine ring of ATP is a part of the hydrophobic stack formed by the amino acid side chains

Summary

Introduction

Phosphorylation is a ubiquitous means of changing a protein’s behavior. Adding a phosphate group to a serine, threonine, or tyrosine amino acid alters the shape and charge of the protein, a change that may activate an enzyme, promote membrane translocation, or trigger binding to DNA. Confirming the Importance of the R-Spine: New Insights into Protein Kinase Regulation The requirements of rational drug design, as well as pure human curiosity, have led researchers to try to understand the structural features of protein kinases that contribute to their regulation.

Results

Conclusion