Defining the conserved internal architecture of a protein kinase

Biochim Biophys Acta. 2010 Mar;1804(3):440-4. doi: 10.1016/j.bbapap.2009.10.017. Epub 2009 Oct 29.


Protein kinases constitute a large protein family of important regulators in all eukaryotic cells. All of the protein kinases have a similar bilobal fold, and their key structural features have been well studied. However, the recent discovery of non-contiguous hydrophobic ensembles inside the protein kinase core shed new light on the internal organization of these molecules. Two hydrophobic "spines" traverse both lobes of the protein kinase molecule, providing a firm but flexible connection between its key elements. The spine model introduces a useful framework for analysis of intramolecular communications, molecular dynamics, and drug design.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Humans
  • Hydrophobic and Hydrophilic Interactions
  • Models, Molecular*
  • Protein Folding*
  • Protein Kinases / chemistry*
  • Protein Structure, Tertiary / physiology


  • Protein Kinases