1nfa
From Proteopedia
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- | [[Image:1nfa.gif|left|200px]] | + | [[Image:1nfa.gif|left|200px]] |
- | + | ||
- | '''HUMAN TRANSCRIPTION FACTOR NFATC DNA BINDING DOMAIN, NMR, 10 STRUCTURES''' | + | {{Structure |
+ | |PDB= 1nfa |SIZE=350|CAPTION= <scene name='initialview01'>1nfa</scene> | ||
+ | |SITE= | ||
+ | |LIGAND= | ||
+ | |ACTIVITY= | ||
+ | |GENE= NFATC1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
+ | }} | ||
+ | |||
+ | '''HUMAN TRANSCRIPTION FACTOR NFATC DNA BINDING DOMAIN, NMR, 10 STRUCTURES''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1NFA is a [ | + | 1NFA is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1NFA OCA]. |
==Reference== | ==Reference== | ||
- | Unusual Rel-like architecture in the DNA-binding domain of the transcription factor NFATc., Wolfe SA, Zhou P, Dotsch V, Chen L, You A, Ho SN, Crabtree GR, Wagner G, Verdine GL, Nature. 1997 Jan 9;385(6612):172-6. PMID:[http:// | + | Unusual Rel-like architecture in the DNA-binding domain of the transcription factor NFATc., Wolfe SA, Zhou P, Dotsch V, Chen L, You A, Ho SN, Crabtree GR, Wagner G, Verdine GL, Nature. 1997 Jan 9;385(6612):172-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8990122 8990122] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transcription regulation]] | [[Category: transcription regulation]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:56:07 2008'' |
Revision as of 10:56, 20 March 2008
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Gene: | NFATC1 (Homo sapiens) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
HUMAN TRANSCRIPTION FACTOR NFATC DNA BINDING DOMAIN, NMR, 10 STRUCTURES
Overview
Transcription factors of the NFAT family regulate the production of effector proteins that coordinate the immune response. The immunosuppressive drugs FK506 and cyclosporin A (CsA) act by blocking a Ca2+-mediated signalling pathway leading to NFAT. Although FK506 and CsA have enabled human organs to be transplanted routinely, the toxic side-effects of these drugs limit their usage. This toxicity might be absent in antagonists that target NFAT directly. As a first step in the structure-based search for NFAT antagonists, we now report the identification and solution structure of a 20K domain of NFATc (NFATc-DBD) that is both necessary and sufficient to bind DNA and activate transcription cooperatively. Although the overall fold of the NFATc DNA-binding domain is related to that of NF-kappaB p50 (refs 2, 3), the two proteins use significantly different strategies for DNA recognition. On the basis of these results, we present a model for the cooperative complex formed between NFAT and the mitogenic transcription factor AP-1 on the interleukin-2 enhancer.
About this Structure
1NFA is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Unusual Rel-like architecture in the DNA-binding domain of the transcription factor NFATc., Wolfe SA, Zhou P, Dotsch V, Chen L, You A, Ho SN, Crabtree GR, Wagner G, Verdine GL, Nature. 1997 Jan 9;385(6612):172-6. PMID:8990122
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