1a02: Difference between revisions
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Revision as of 14:38, 12 November 2007
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STRUCTURE OF THE DNA BINDING DOMAINS OF NFAT, FOS AND JUN BOUND TO DNA
OverviewOverview
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.
DiseaseDisease
Known diseases associated with this structure: Autoimmune polyglandular disease, type I OMIM:[607358], Sveinsson choreoretinal atrophy OMIM:[189967]
About this StructureAbout this Structure
1A02 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
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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