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Sci. STKE, 17 May 2005
Vol. 2005, Issue 284, p. pe23
[DOI: 10.1126/stke.2842005pe23]
PERSPECTIVES
A Rationally Designed Small Molecule That Inhibits the HIF-1–ARNT Heterodimer from Binding to DNA in Vivo
Charles Vinson
Laboratory of Metabolism, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA.
Summary:
Modern drug development is focused on two steps: the identification of new molecular targets and the development of drugs that affect these targets. A molecular target can be an enzymatic activity or a macromolecular interface that is important in a disease pathway. Current drugs on the market are biased toward targeting cell surface receptors and intracellular enzymatic activities. However, macromolecular interfaces can also serve as potential molecular targets. A recent paper from Kaelin and Dervan's groups examined an underused molecular target—transcription factor DNA binding. To specifically disrupt transcriptional activation, they used a rationally designed small molecule that binds specifically in the minor groove of a DNA sequence that in vivo is bound by a bHLH heterodimer transcription factor.
Citation: C. Vinson, A Rationally Designed Small Molecule That Inhibits the HIF-1–ARNT Heterodimer from Binding to DNA in Vivo. Sci. STKE2005, pe23 (2005).
–ARNT Heterodimer from Binding to DNA in Vivo
–ARNT Heterodimer from Binding to DNA in Vivo. Sci. STKE 2005, pe23 (2005).
