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

Defining the conserved internal architecture of a protein kinase.

Author information

1
Howard Hughes Medical Institute, University of California at San Diego, 9500 Gilman Drive, La Jolla, CA 92093, USA.

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.

PMID:
19879387
PMCID:
PMC3435107
DOI:
10.1016/j.bbapap.2009.10.017
[Indexed for MEDLINE]
Free PMC Article

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