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1a66
From Proteopedia
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==Overview== | ==Overview== | ||
| - | The nuclear factor of the activated T cell (NFAT) family of transcription | + | The nuclear factor of the activated T cell (NFAT) family of transcription factors regulates cytokine gene expression by binding to the promoter/enhancer regions of antigen-responsive genes, usually in cooperation with heterologous DNA-binding partners. Here we report the solution structure of the binary complex formed between the core DNA-binding domain of human NFATC1 and the ARRE2 DNA site from the interleukin-2 promoter. The structure reveals that DNA binding induces the folding of key structural elements that are required for both sequence-specific recognition and the establishment of cooperative protein-protein contacts. The orientation of the NFAT DNA-binding domain observed in the binary NFATC1-DBD*/ DNA complex is distinct from that seen in the ternary NFATC2/AP-1/DNA complex, suggesting that the domain reorients upon formation of a cooperative transcriptional complex. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Doetsch, V.]] | [[Category: Doetsch, V.]] | ||
| - | [[Category: Sun, L | + | [[Category: Sun, L J.]] |
| - | [[Category: Verdine, G | + | [[Category: Verdine, G L.]] |
[[Category: Wagner, G.]] | [[Category: Wagner, G.]] | ||
[[Category: Zhou, P.]] | [[Category: Zhou, P.]] | ||
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[[Category: transcription factor]] | [[Category: transcription factor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:41:21 2008'' |
Revision as of 09:41, 21 February 2008
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SOLUTION NMR STRUCTURE OF THE CORE NFATC1/DNA COMPLEX, 18 STRUCTURES
Overview
The nuclear factor of the activated T cell (NFAT) family of transcription factors regulates cytokine gene expression by binding to the promoter/enhancer regions of antigen-responsive genes, usually in cooperation with heterologous DNA-binding partners. Here we report the solution structure of the binary complex formed between the core DNA-binding domain of human NFATC1 and the ARRE2 DNA site from the interleukin-2 promoter. The structure reveals that DNA binding induces the folding of key structural elements that are required for both sequence-specific recognition and the establishment of cooperative protein-protein contacts. The orientation of the NFAT DNA-binding domain observed in the binary NFATC1-DBD*/ DNA complex is distinct from that seen in the ternary NFATC2/AP-1/DNA complex, suggesting that the domain reorients upon formation of a cooperative transcriptional complex.
About this Structure
1A66 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Solution structure of the core NFATC1/DNA complex., Zhou P, Sun LJ, Dotsch V, Wagner G, Verdine GL, Cell. 1998 Mar 6;92(5):687-96. PMID:9506523
Page seeded by OCA on Thu Feb 21 11:41:21 2008
Categories: Homo sapiens | Single protein | Doetsch, V. | Sun, L J. | Verdine, G L. | Wagner, G. | Zhou, P. | Arre2 | Binary | Binary complex | Complex | Enhanceosome | Il-2 | Nfat | Nfat/dna | Nfat2 | Nfatc | Nfatc1 | Nfatc1/dna | Nmr | Rel | Transcription factor
