1: J Mol Biol. 2003 Dec 12;334(5):1009-22. 

Structure of NFAT bound to DNA as a monomer.

Stroud JC, Chen L.

Department of Chemistry and Biochemistry, University of Colorado at Boulder,
Campus Box 215, Boulder, CO 80309-0437, USA.

The nuclear factor of activated T cells (NFAT) is a calcium-dependent
transcription factor that cooperates with a myriad of partner transcription
factors to regulate distinct transcription programs. Transcription activation by
NFAT without the cooperation of co-stimulatory signals in lymphocytes can also
impose a genetic program of anergy. Although the ternary NFAT1/Fos-Jun/DNA
complex has been structurally characterized, how NFAT1 recognizes DNA in the
absence of cooperative partners and how such a binary NFAT/DNA complex may lead
to the assembly of distinct high-order NFAT transcription complexes are still
poorly understood. We have determined the crystal structure of the entire Rel
homology region (RHR) of human NFAT1 (NFATc2) bound to DNA as a monomer. We also
present footprinting evidence that corroborates the protein-DNA contacts
observed in the crystal structure. Our structural and biochemical studies reveal
the mechanism by which the monomeric Rel protein NFAT recognizes its cognate DNA
site. A remarkable feature of the binary NFAT/DNA complex is the conformational
flexibility exhibited by NFAT1 in the four independent copies of the NFAT/DNA
complex in the crystal structure, which may reflect a mechanism by which NFAT1
interacts with a variety of protein partners as it mediates disparate biological
responses.

PMID: 14643663 [PubMed - indexed for MEDLINE]


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