1PZU

An asymmetric NFAT1-RHR homodimer on a pseudo-palindromic, Kappa-B site

Summary for 1PZU

• Entry DOI: 10.2210/pdb1pzu/pdb
• Related: 1A02
• Descriptor: 5'-D(*TP*TP*GP*AP*GP*GP*AP*AP*TP*TP*TP*CP*CP*A)-3', 5'-D(*AP*AP*TP*GP*GP*AP*AP*AP*TP*TP*CP*CP*TP*C)-3', Nuclear factor of activated T-cells, cytoplasmic 2 (3 entities in total)
• Functional Keywords: transcription factor, nfat1-rhr homodimer, protein-dna complex, human il8 promoter, transcription-dna complex, transcription/dna
• Biological source: Homo sapiens (human)
• Cellular location: Cytoplasm: Q13469
• Total number of polymer chains: 12
• Total formula weight: 231301.24

Authors

Jin, L.,Sliz, P.,Chen, L.,Macian, F.,Rao, A.,Hogan, P.G.,Harrison, S.C. (deposition date: 2003-07-14, release date: 2003-09-09, Last modification date: 2024-02-21)

Primary citation

Jin, L.,Sliz, P.,Chen, L.,Macian, F.,Rao, A.,Hogan, P.G.,Harrison, S.C.
An asymmetric NFAT1 dimer on a pseudo-palindromic KB-like DNA site
Nat.Struct.Biol., 10:807-811, 2003

PubMed Abstract: The crystal structure of the NFAT1 Rel homology region (RHR) bound to a pseudo-palindromic DNA site reveals an asymmetric dimer interaction between the RHR-C domains, unrelated to the contact seen in Rel dimers such as NF kappa B. Binding studies with a form of the NFAT1 RHR defective in the dimer contact show loss of cooperativity and demonstrate that the same interaction is present in solution. The structure we have determined may correspond to a functional NFAT binding mode at palindromic sites of genes induced during the anergic response to weak TCR signaling.

PubMed: 12949491
DOI: 10.1038/nsb975

Experimental method

X-RAY DIFFRACTION (3.1 Å)