STAT proteins are a family of eukaryotic transcription factors that me
diate 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 specif
ic 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 Angstrom resolution. The structure provides insight into the v
arious steps by which STAT proteins deliver a response signal directly
from the cell membrane to their target genes in the nucleus.