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

• Published in: Nature structural biology Vol. 10; no. 10; pp. 807 - 811
• Main Authors: Harrison, Stephen C, Jin, Lei, Sliz, Piotr, Chen, Lin, Macián, Fernando, Rao, Anjana, Hogan, Patrick G
• Format: Journal Article
• Language: English
• Published: United States 01-10-2003
• Subjects: Dimerization; DNA - metabolism; DNA-Binding Proteins - chemistry; DNA-Binding Proteins - metabolism; Humans; NFAT1 protein; NFATC Transcription Factors; Nuclear Proteins; Protein Structure, Tertiary; Transcription Factors - chemistry; Transcription Factors - metabolism
• ISSN: 1072-8368; 2331-365X
• DOI: 10.1038/nsb975

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.