1p7h is a 8 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
↑ Giffin MJ, Stroud JC, Bates DL, von Koenig KD, Hardin J, Chen L. Structure of NFAT1 bound as a dimer to the HIV-1 LTR kappa B element. Nat Struct Biol. 2003 Oct;10(10):800-6. Epub 2003 Aug 31. PMID:12949493 doi:http://dx.doi.org/10.1038/nsb981
