1P7H

Structure of NFAT1 bound as a dimer to the HIV-1 LTR kB element

Summary for 1P7H

• Entry DOI: 10.2210/pdb1p7h/pdb
• Descriptor: 5'-D(*AP*AP*TP*GP*GP*GP*GP*AP*CP*TP*TP*TP*CP*CP*A)-3', 5'-D(*TP*TP*TP*GP*GP*AP*AP*AP*GP*TP*CP*CP*CP*CP*A)-3', Nuclear factor of activated T-cells, cytoplasmic 2, ... (4 entities in total)
• Functional Keywords: dna binding protein, transcription regulation, activator, transcription-dna complex, transcription/dna
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: Q13469
• Total number of polymer chains: 8
• Total formula weight: 148303.90

Authors

Giffin, M.J.,Stroud, J.C.,Bates, D.L.,von Koenig, K.D.,Hardin, J.,Chen, L. (deposition date: 2003-05-01, release date: 2003-09-23, Last modification date: 2024-02-14)

Primary citation

Giffin, M.J.,Stroud, J.C.,Bates, D.L.,von Koenig, K.D.,Hardin, J.,Chen, L.
Structure of NFAT1 bound as a dimer to the HIV-1 LTR kappa B element
Nat.Struct.Biol., 10:800-806, 2003

PubMed Abstract: 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.

PubMed: 12949493
DOI: 10.1038/nsb981

Experimental method

X-RAY DIFFRACTION (2.6 Å)