title: Defining the conserved internal architecture of a protein kinase.
abstract: 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.
authors.affiliation: Howard Hughes Medical Institute, University of California at San Diego, 9500 Gilman Drive, La Jolla, CA 92093, USA.
authors.forename: Alexandr P
authors.initials: AP
authors.lastname: Kornev
authors.forename: Susan S
authors.initials: SS
authors.lastname: Taylor
mesh_terms: D000818:Animals; D006801:Humans; D057927:Hydrophobic and Hydrophilic Interactions; D008958:Models, Molecular; D017510:Protein Folding; D011494:Protein Kinases / Q000737:chemistry*; D017434:Protein Structure, Tertiary / Q000502:physiology
chemical_list: D011494:Protein Kinases