1OWR

CRYSTAL STRUCTURE OF HUMAN NFAT1 BOUND MONOMERICALLY TO DNA

Summary for 1OWR

• Entry DOI: 10.2210/pdb1owr/pdb
• Related: 1A02
• Descriptor: NFAT1 Monomeric Binding Site, Plus Strand, NFAT1 Monomeric Binding Site, Minus Strand, Nuclear factor of activated T-cells, cytoplasmic 2 (3 entities in total)
• Functional Keywords: beta barrel, protein-dna complex, double helix, binary, monomer, pseudo-continuous, transcription-dna complex, transcription/dna
• Biological source: Homo sapiens (human); More
• Cellular location: Cytoplasm: Q13469
• Total number of polymer chains: 12
• Total formula weight: 165955.35

Authors

Stroud, J.C.,Chen, L. (deposition date: 2003-03-29, release date: 2004-02-10, Last modification date: 2023-08-16)

Primary citation

Stroud, J.C.,Chen, L.
Structure of NFAT Bound to DNA as a Monomer
J.Mol.Biol., 334:1009-1022, 2003

PubMed Abstract: 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.

PubMed: 14643663
DOI: 10.1016/j.jmb.2003.09.065

Experimental method

X-RAY DIFFRACTION (3 Å)