1imh
From Proteopedia
(New page: 200px<br /> <applet load="1imh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1imh, resolution 2.86Å" /> '''TonEBP/DNA COMPLEX'...) |
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| - | [[Image:1imh.gif|left|200px]]<br /> | + | [[Image:1imh.gif|left|200px]]<br /><applet load="1imh" size="350" color="white" frame="true" align="right" spinBox="true" |
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caption="1imh, resolution 2.86Å" /> | caption="1imh, resolution 2.86Å" /> | ||
'''TonEBP/DNA COMPLEX'''<br /> | '''TonEBP/DNA COMPLEX'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Tonicity-responsive enhancer binding protein (TonEBP), also known as | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1IMH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | + | 1IMH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IMH OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Lopez-Rodriguez, C.]] | [[Category: Lopez-Rodriguez, C.]] | ||
[[Category: Rao, A.]] | [[Category: Rao, A.]] | ||
| - | [[Category: Stroud, J | + | [[Category: Stroud, J C.]] |
[[Category: beta barrel]] | [[Category: beta barrel]] | ||
[[Category: dna encirclement]] | [[Category: dna encirclement]] | ||
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[[Category: protein-dna complex]] | [[Category: protein-dna complex]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:13:21 2008'' |
Revision as of 11:13, 21 February 2008
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TonEBP/DNA COMPLEX
Overview
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.
About this Structure
1IMH is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of a TonEBP-DNA complex reveals DNA encircled by a transcription factor., Stroud JC, Lopez-Rodriguez C, Rao A, Chen L, Nat Struct Biol. 2002 Feb;9(2):90-4. PMID:11780147
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