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| - | [[Image:1owr.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1owr.png|left|200px]] |
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| | {{STRUCTURE_1owr| PDB=1owr | SCENE= }} | | {{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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| - | ==Overview==
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| - | 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. | + | The line below this paragraph, {{ABSTRACT_PUBMED_14643663}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 14643663 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_14643663}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Protein-dna complex]] | | [[Category: Protein-dna complex]] |
| | [[Category: Pseudo-continuous]] | | [[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 Mon Jul 28 08:44:36 2008'' |
Revision as of 05:44, 28 July 2008
Template:STRUCTURE 1owr
CRYSTAL STRUCTURE OF HUMAN NFAT1 BOUND MONOMERICALLY TO DNA
Template:ABSTRACT PUBMED 14643663
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 Jul 28 08:44:36 2008
