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of outstanding interest. GABP is a transcriptional activator from the mouse composed of two subunits: GABPα, which contains an ETS DNA-binding domain, and GABPβ, which contains a set of 412 ankyrin repeats. The structure of a GABPα/β heterodimer bound to DNA, determined at a resolution of 2.15 Å, shows that the ankyrin repeats all contact GABPα using the tips of the long loop found in each repeat. The ankyrin repeats contact both the ETS domain of GABPα and a carboxy-terminal extension required for heterodimerization. All DNA contacts are mediated by GABPα.
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of outstanding interest. Previous studies of Rel homology region proteins had been of the p50 and p65 homodimers. The structure of the p50/P65 heterodimer, the formation of which is preferred over that of the homodimers, reveals the set of dimer interactions responsible for the heterodimer's enhanced stability.
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of outstanding interest. The structure of the NFAT rel homology region protein bound to the Fos-Jun bZIP heterodimer and DNA is the most complex structure to date of a multicomponent protein-DNA complex involved in transcriptional regulation. As compared with the structure of the Fos-Jun heterodimer alone bound to DNA [2], the coiled-coil region of Fos-Jun bends towards NFAT. The DNA bends as well, thereby bringing the proteins close enough to form extensive contacts.
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