An asymmetric NFAT1 dimer on a pseudo-palindromic κB-like DNA site

Lei Jin, Piotr Sliz, Lin Chen, Fernando Macián, Anjana Rao, Patrick G. Hogan, Stephen C. Harrison

Research output: Contribution to journalArticlepeer-review

55 Scopus citations


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 NFκB. 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.

Original languageEnglish (US)
Pages (from-to)807-811
Number of pages5
JournalNature Structural Biology
Issue number10
StatePublished - Oct 1 2003

ASJC Scopus subject areas

  • Structural Biology
  • Biochemistry
  • Genetics


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