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1owr
From Proteopedia
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(New page: 200px<br /> <applet load="1owr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1owr, resolution 3.00Å" /> '''CRYSTAL STRUCTURE O...)
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Revision as of 16:31, 12 November 2007
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CRYSTAL STRUCTURE OF HUMAN NFAT1 BOUND MONOMERICALLY TO DNA
Overview
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.
About this Structure
1OWR is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of NFAT bound to DNA as a monomer., Stroud JC, Chen L, J Mol Biol. 2003 Dec 12;334(5):1009-22. PMID:14643663
Page seeded by OCA on Mon Nov 12 18:37:44 2007
