TRANSCRIPTION FACTOR STAT3B/DNA COMPLEXTRANSCRIPTION FACTOR STAT3B/DNA COMPLEX

Structural highlights

1bg1 is a 2 chain structure with sequence from Mus musculus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.25Å
Ligands:
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

STAT3_MOUSE Signal transducer and transcription activator that mediates cellular responses to interleukins, KITLG/SCF and other growth factors. May mediate cellular responses to activated FGFR1, FGFR2, FGFR3 and FGFR4. Binds to the interleukin-6 (IL-6)-responsive elements identified in the promoters of various acute-phase protein genes. Activated by IL31 through IL31RA. STAT3B interacts with the N-terminal part of JUN to activate such promoters in a cooperative way.[1]

Evolutionary Conservation

 

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

STAT proteins are a family of eukaryotic transcription factors that mediate the response to a large number of cytokines and growth factors. Upon activation by cell-surface receptors or their associated kinases, STAT proteins dimerize, translocate to the nucleus and bind to specific promoter sequences on their target genes. Here we report the first crystal structure of a STAT protein bound to its DNA recognition site at 2.25 A resolution. The structure provides insight into the various steps by which STAT proteins deliver a response signal directly from the cell membrane to their target genes in the nucleus.

Three-dimensional structure of the Stat3beta homodimer bound to DNA.,Becker S, Groner B, Muller CW Nature. 1998 Jul 9;394(6689):145-51. PMID:9671298[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Hart KC, Robertson SC, Donoghue DJ. Identification of tyrosine residues in constitutively activated fibroblast growth factor receptor 3 involved in mitogenesis, Stat activation, and phosphatidylinositol 3-kinase activation. Mol Biol Cell. 2001 Apr;12(4):931-42. PMID:11294897
  2. Becker S, Groner B, Muller CW. Three-dimensional structure of the Stat3beta homodimer bound to DNA. Nature. 1998 Jul 9;394(6689):145-51. PMID:9671298 doi:10.1038/28101

1bg1, resolution 2.25Å

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