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1p7h
From Proteopedia
(New page: 200px<br /> <applet load="1p7h" size="450" color="white" frame="true" align="right" spinBox="true" caption="1p7h, resolution 2.60Å" /> '''Structure of NFAT1 ...) |
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Revision as of 16:34, 12 November 2007
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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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