Three-dimensional structure of the Stat3β homodimer bound to DNA

Stefan Becker, Bernd Groner and Christoph W. Müller ()
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Stefan Becker: European Molecular Biology Laboratory, Grenoble Outstation
Bernd Groner: Institute for Experimental Cancer Research, Tumor Biology Center
Christoph W. Müller: European Molecular Biology Laboratory, Grenoble Outstation

Nature, 1998, vol. 394, issue 6689, 145-151

Abstract: Abstract STAT proteins are a family of eukaryotic transcription factors that mediate the response to a large number of cytokines and growth factors. Upon activation by cell-surface receptors or their associated kinases, STAT proteins dimerize, translocate to the nucleus and bind to specific promoter sequences on their target genes. Here we report the first crystal structure of a STAT protein bound to its DNA recognition site at 2.25 Å resolution. The structure provides insight into the various steps by which STAT proteins deliver a response signal directly from the cell membrane to their target genes in the nucleus.

Date: 1998
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Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:394:y:1998:i:6689:d:10.1038_28101

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DOI: 10.1038/28101

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