1owr
From Proteopedia
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[[Image:1owr.gif|left|200px]] | [[Image:1owr.gif|left|200px]] | ||
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| - | + | {{STRUCTURE_1owr| PDB=1owr | SCENE= }} | |
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'''CRYSTAL STRUCTURE OF HUMAN NFAT1 BOUND MONOMERICALLY TO DNA''' | '''CRYSTAL STRUCTURE OF HUMAN NFAT1 BOUND MONOMERICALLY TO DNA''' | ||
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[[Category: Chen, L.]] | [[Category: Chen, L.]] | ||
[[Category: Stroud, J C.]] | [[Category: Stroud, J C.]] | ||
| - | [[Category: | + | [[Category: Beta barrel]] |
| - | [[Category: | + | [[Category: Binary]] |
| - | [[Category: | + | [[Category: Double helix]] |
| - | [[Category: | + | [[Category: Monomer]] |
| - | [[Category: | + | [[Category: Protein-dna complex]] |
| - | [[Category: | + | [[Category: Pseudo-continuous]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:22:35 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 01:22, 3 May 2008
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 Sat May 3 04:22:35 2008
