Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
1926605 | Archives of Biochemistry and Biophysics | 2008 | 7 Pages |
Abstract
A series of small molecule, ATP-competitive phosphoinositide 3-kinase inhibitors have been examined in homology models of the four class I isoforms, p110α, p110β, p110δ and p110γ. This analysis provided an insight into the mode of binding of these inhibitors to the hinge and to other key regions of the ATP binding site in each of the four subtypes. Significantly, residues were identified that differ between these proteins, and which help explain the isoform-selective inhibition profiles of the compounds.
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Authors
Marketa J. Zvelebil, Michael D. Waterfield, Stephen J. Shuttleworth,