1p7h
From Proteopedia
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| - | [[Image:1p7h.gif|left|200px]]<br /> | + | [[Image:1p7h.gif|left|200px]]<br /><applet load="1p7h" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1p7h" size=" | + | |
caption="1p7h, resolution 2.60Å" /> | caption="1p7h, resolution 2.60Å" /> | ||
'''Structure of NFAT1 bound as a dimer to the HIV-1 LTR kB element'''<br /> | '''Structure of NFAT1 bound as a dimer to the HIV-1 LTR kB element'''<br /> | ||
==Overview== | ==Overview== | ||
| - | DNA binding by NFAT1 as a dimer has been implicated in the activation of | + | DNA binding by NFAT1 as a dimer has been implicated in the activation of host and viral genes. Here we report a crystal structure of NFAT1 bound cooperatively as a dimer to the highly conserved kappa B site from the human immunodeficiency virus 1 (HIV-1) long terminal repeat (LTR). This structure reveals a new mode of dimerization and protein-DNA recognition by the Rel homology region (RHR) of NFAT1. The two NFAT1 monomers form a complete circle around the kappa B DNA through protein-protein interactions mediated by both their N- and C-terminal subdomains. The major dimer interface, formed by the C-terminal domain, is asymmetric and substantially different from the symmetric dimer interface seen in other Rel family proteins. Comparison to other NFAT structures, including NFAT5 and the NFAT1-Fos-Jun-ARRE2 complex, reveals that NFAT1 adopts different conformations and its protein surfaces mediate distinct protein-protein interactions in the context of different DNA sites. |
==About this Structure== | ==About this Structure== | ||
| - | 1P7H 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:// | + | 1P7H 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=1P7H OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Bates, D | + | [[Category: Bates, D L.]] |
[[Category: Chen, L.]] | [[Category: Chen, L.]] | ||
| - | [[Category: Giffin, M | + | [[Category: Giffin, M J.]] |
[[Category: Hardin, J.]] | [[Category: Hardin, J.]] | ||
| - | [[Category: Koenig, K | + | [[Category: Koenig, K D.von.]] |
| - | [[Category: Stroud, J | + | [[Category: Stroud, J C.]] |
[[Category: activator]] | [[Category: activator]] | ||
[[Category: dna binding protein]] | [[Category: dna binding protein]] | ||
[[Category: transcription regulation]] | [[Category: transcription regulation]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:25:58 2008'' |
Revision as of 12:26, 21 February 2008
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Structure of NFAT1 bound as a dimer to the HIV-1 LTR kB element
Overview
DNA binding by NFAT1 as a dimer has been implicated in the activation of host and viral genes. Here we report a crystal structure of NFAT1 bound cooperatively as a dimer to the highly conserved kappa B site from the human immunodeficiency virus 1 (HIV-1) long terminal repeat (LTR). This structure reveals a new mode of dimerization and protein-DNA recognition by the Rel homology region (RHR) of NFAT1. The two NFAT1 monomers form a complete circle around the kappa B DNA through protein-protein interactions mediated by both their N- and C-terminal subdomains. The major dimer interface, formed by the C-terminal domain, is asymmetric and substantially different from the symmetric dimer interface seen in other Rel family proteins. Comparison to other NFAT structures, including NFAT5 and the NFAT1-Fos-Jun-ARRE2 complex, reveals that NFAT1 adopts different conformations and its protein surfaces mediate distinct protein-protein interactions in the context of different DNA sites.
About this Structure
1P7H is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of NFAT1 bound as a dimer to the HIV-1 LTR kappa B element., Giffin MJ, Stroud JC, Bates DL, von Koenig KD, Hardin J, Chen L, Nat Struct Biol. 2003 Oct;10(10):800-6. Epub 2003 Aug 31. PMID:12949493
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