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 Cited by 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: 14643663DOI: 10.1016/j.jmb.2003.09.065 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3 Å) |
Structure validation
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