PDBsum entry 1bg1

Transcription/DNA

PDB id: 1bg1

Contents

Protein chain

559 a.a. *

DNA/RNA

Waters ×154

* Residue conservation analysis

References listed in PDB file

Key reference

Title

Three-Dimensional structure of the stat3beta homodimer bound to DNA.

Authors

S.Becker, B.Groner, C.W.Müller.

Ref.

Nature, 1998, 394, 145-151. [DOI no: 10.1038/28101]

PubMed id

9671298

Abstract

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.

Figure 2.
Figure 2 Ribbon diagram of the Stat3 homodimer-DNA complex. The N-terminal 4-helix bundle is shown in blue, the -barrel domain in red, the connector domain in green, and the SH2 domain and phosphotyrosine-containing region in yellow. Disordered regions between helices 1 and 2 and residues 689 to 701 have been modelled in grey. This figure and Fig. 3b were produced with program RIBBONS45. Views are shown a, along the DNA axis (the dyad of the complex running vertically); b, from the side, with monomer 2 depicted in grey; and c, from the top. Phosphotyrosines are indicated by a Y in c.

Figure 4.
Figure 4 Binding of the phosphotyrosine peptides by the C-terminal SH2 domains. Carbon atoms of the phosphotyrosine peptide covalently linked to monomer I and monomer II are yellow and white, respectively. Produced with program GRASP46.

The above figures are reprinted by permission from Macmillan Publishers Ltd: Nature (1998, 394, 145-151) copyright 1998.