Summary information and primary citation
- PDB-id
-
1imh;
SNAP-derived features in text and
JSON formats
- Class
- transcription-DNA
- Method
- X-ray (2.86 Å)
- Summary
- Tonebp-DNA complex
- Reference
-
Stroud JC, Lopez-Rodriguez C, Rao A, Chen L (2002):
"Structure
of a TonEBP-DNA complex reveals DNA encircled by a
transcription factor." Nat.Struct.Biol.,
9, 90-94. doi: 10.1038/nsb749.
- Abstract
- Tonicity-responsive enhancer binding protein (TonEBP),
also known as NFAT5, is a unique member of the NFAT family
of transcription factors that regulates gene expression
induced by osmotic stress in mammalian cells. Unlike
monomeric members of the NFAT family, TonEBP exists as a
homodimer and binds asymmetric TonE DNA sites; furthermore,
the affinity of TonEBP for DNA is much lower than that of
other NFAT proteins. How TonEBP recognizes the TonE site
and regulates the activation of hypertonicity response
genes has not been clear. Here we show that TonEBP adopts a
NF-kappaB-like structure upon binding to DNA, providing a
direct structural link between the NFAT and NF-kappaB
family of transcription factors. We also show that TonEBP
completely encircles its DNA target and present biochemical
evidence that the DNA encirclement may lead to increased
kinetic stability of the TonEBP-DNA complex. Thus, the list
of proteins that bind DNA by encirclement is now expanded
to include sequence-specific transcription factors.
