1a02
From Proteopedia
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- | [[Image:1a02.gif|left|200px]] | + | [[Image:1a02.gif|left|200px]] |
- | + | ||
- | '''STRUCTURE OF THE DNA BINDING DOMAINS OF NFAT, FOS AND JUN BOUND TO DNA''' | + | {{Structure |
+ | |PDB= 1a02 |SIZE=350|CAPTION= <scene name='initialview01'>1a02</scene>, resolution 2.700Å | ||
+ | |SITE= | ||
+ | |LIGAND= | ||
+ | |ACTIVITY= | ||
+ | |GENE= NFAT1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | ||
+ | }} | ||
+ | |||
+ | '''STRUCTURE OF THE DNA BINDING DOMAINS OF NFAT, FOS AND JUN BOUND TO DNA''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1A02 is a [ | + | 1A02 is a [[Protein complex]] structure of sequences 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=1A02 OCA]. |
==Reference== | ==Reference== | ||
- | Structure of the DNA-binding domains from NFAT, Fos and Jun bound specifically to DNA., Chen L, Glover JN, Hogan PG, Rao A, Harrison SC, Nature. 1998 Mar 5;392(6671):42-8. PMID:[http:// | + | Structure of the DNA-binding domains from NFAT, Fos and Jun bound specifically to DNA., Chen L, Glover JN, Hogan PG, Rao A, Harrison SC, Nature. 1998 Mar 5;392(6671):42-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9510247 9510247] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: transcription synergy]] | [[Category: transcription synergy]] | ||
- | ''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 09:50:57 2008'' |
Revision as of 07:50, 20 March 2008
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, resolution 2.700Å | |||||||
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Gene: | NFAT1 (Homo sapiens) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
STRUCTURE OF THE DNA BINDING DOMAINS OF NFAT, FOS AND JUN BOUND TO DNA
Contents |
Overview
The nuclear factor of activated T cells (NFAT) and the AP-1 heterodimer, Fos-Jun, cooperatively bind a composite DNA site and synergistically activate the expression of many immune-response genes. A 2.7-A-resolution crystal structure of the DNA-binding domains of NFAT, Fos and Jun, in a quaternary complex with a DNA fragment containing the distal antigen-receptor response element from the interleukin-2 gene promoter, shows an extended interface between NFAT and AP-1, facilitated by the bending of Fos and DNA. The tight association of the three proteins on DNA creates a continuous groove for the recognition of 15 base pairs.
Disease
Known diseases associated with this structure: Autoimmune polyglandular disease, type I OMIM:[607358], Sveinsson choreoretinal atrophy OMIM:[189967]
About this Structure
1A02 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structure of the DNA-binding domains from NFAT, Fos and Jun bound specifically to DNA., Chen L, Glover JN, Hogan PG, Rao A, Harrison SC, Nature. 1998 Mar 5;392(6671):42-8. PMID:9510247
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