2ghg

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Revision as of 23:12, 12 November 2007 by OCA (talk | contribs) (New page: left|200px<br /> <applet load="2ghg" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ghg, resolution 3.50Å" /> '''h-CHK1 complexed wi...)
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File:2ghg.gif


2ghg, resolution 3.50Å

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h-CHK1 complexed with A431994

OverviewOverview

We describe a series of potent and selective oxindole-pyridine-based, protein kinase B/Akt inhibitors. The most potent compound 11n in this, series demonstrated an IC(50) of 0.17nM against Akt1 and more than, 100-fold selectivity over other Akt isozymes. The selectivity against, other protein kinases was highly dependent on the C-3 substitutions at the, oxindole scaffold, with unsubstituted 9e or 3-furan-2-ylmethylene (11n), more selective and 3-(1H-pyrrol-2-yl)methylene (11f) or, 3-(1H-imidazol-2-yl)methylene (11k) less selective. In a mouse xenograft, model, 9d, 11f, and 11n inhibited tumor growth but with accompanying, toxicity.

About this StructureAbout this Structure

2GHG is a Single protein structure of sequence from Homo sapiens with A53 as ligand. Active as Non-specific serine/threonine protein kinase, with EC number 2.7.11.1 Full crystallographic information is available from OCA.

ReferenceReference

Discovery and SAR of oxindole-pyridine-based protein kinase B/Akt inhibitors for treating cancers., Zhu GD, Gandhi VB, Gong J, Luo Y, Liu X, Shi Y, Guan R, Magnone SR, Klinghofer V, Johnson EF, Bouska J, Shoemaker A, Oleksijew A, Jarvis K, Park C, Jong RD, Oltersdorf T, Li Q, Rosenberg SH, Giranda VL, Bioorg Med Chem Lett. 2006 Jul 1;16(13):3424-9. Epub 2006 Apr 27. PMID:16644221

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