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1A02

STRUCTURE OF THE DNA BINDING DOMAINS OF NFAT, FOS AND JUN BOUND TO DNA

Summary for 1A02
Entry DOI10.2210/pdb1a02/pdb
DescriptorDNA (5'-D(*DTP*DTP*DGP*DGP*DAP*DAP*DAP*DAP*DTP*DTP*DTP*DGP*DTP*DTP*DTP*DCP*DAP*DTP*DAP*DG)-3'), DNA (5'-D(*DAP*DAP*DCP*DTP*DAP*DTP*DGP*DAP*DAP*DAP*DCP*DAP*DAP*DAP*DTP*DTP*DTP*DTP*DCP*DC)-3'), NUCLEAR FACTOR OF ACTIVATED T CELLS, ... (6 entities in total)
Functional Keywordstranscription factor, nfat, nf-at, ap-1, fos-jun, quaternary protein-dna complex, transcription synergy, combinatorial gene regulation, transcription-dna complex, transcription/dna
Biological sourceHomo sapiens (human)
More
Cellular locationCytoplasm: Q13469
Nucleus: P01100 P05412
Total number of polymer chains5
Total formula weight59845.47
Authors
Chen, L.,Glover, J.N.M.,Hogan, P.G.,Rao, A.,Harrison, S.C. (deposition date: 1997-12-08, release date: 1998-05-27, Last modification date: 2024-02-07)
Primary citationChen, L.,Glover, J.N.,Hogan, P.G.,Rao, A.,Harrison, S.C.
Structure of the DNA-binding domains from NFAT, Fos and Jun bound specifically to DNA.
Nature, 392:42-48, 1998
Cited by
PubMed Abstract: 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.
PubMed: 9510247
DOI: 10.1038/32100
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.7 Å)
Structure validation

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数据于2025-06-18公开中

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