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1a02
From Proteopedia
STRUCTURE OF THE DNA BINDING DOMAINS OF NFAT, FOS AND JUN BOUND TO DNA
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.
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
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
About this Structure
1a02 is a 5 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
- Chen L, Glover JN, Hogan PG, Rao A, Harrison SC. Structure of the DNA-binding domains from NFAT, Fos and Jun bound specifically to DNA. Nature. 1998 Mar 5;392(6671):42-8. PMID:9510247 doi:10.1038/32100
- Cokol M, Nair R, Rost B. Finding nuclear localization signals. EMBO Rep. 2000 Nov;1(5):411-5. PMID:11258480 doi:10.1093/embo-reports/kvd092
- Hicks JM, Hsu VL. The extended left-handed helix: a simple nucleic acid-binding motif. Proteins. 2004 May 1;55(2):330-8. PMID:15048824 doi:10.1002/prot.10630
