PDBsum entry 1bf5

Gene regulation/DNA

PDB id: 1bf5

Contents

Protein chain

545 a.a. *

DNA/RNA

* Residue conservation analysis

PDB id:

1bf5

Name:

Gene regulation/DNA

Title:

Tyrosine phosphorylated stat-1/DNA complex

Structure:

DNA (5'- d( Ap Cp Ap Gp Tp Tp Tp Cp Cp Cp Gp Tp Ap Ap Ap Tp G p C)-3'). Chain: b. Engineered: yes. DNA (5'- d( Tp Gp Cp Ap Tp Tp Tp Ap Cp Gp Gp Gp Ap Ap Ap Cp T p G)-3'). Chain: c. Engineered: yes. Signal transducer and activator of transcription 1-

Source:

Homo sapiens. Human. Organism_taxid: 9606. Expressed in: escherichia coli bl21. Expression_system_taxid: 511693. Expressed in: escherichia coli. Expression_system_taxid: 562

Biol. unit:

Dimer (from PDB file)

Resolution:

2.90Å R-factor: 0.227 R-free: 0.293

Authors:

J.Kuriyan,Y.Zhao,X.Chen,U.Vinkemeier,D.Jeruzalmi,J.E.Darnell Jr.

Key ref:

X.Chen et al. (1998). Crystal structure of a tyrosine phosphorylated STAT-1 dimer bound to DNA. Cell, 93, 827-839. PubMed id: 9630226 DOI: 10.1016/S0092-8674(00)81443-9

Date:

27-May-98 Release date: 12-Aug-98

Protein chain

P42224  (STAT1_HUMAN) -  Signal transducer and activator of transcription 1-alpha/beta from Homo sapiens

Seq: 750 a.a.

Struc: 545 a.a.

DNA/RNA chains

A-C-A-G-T-T-T-C-C-C-G-T-A-A-A-T-G-C 18 bases

T-G-C-A-T-T-T-A-C-G-G-G-A-A-A-C-T-G 18 bases

DOI no: 10.1016/S0092-8674(00)81443-9

Cell 93:827-839 (1998)

PubMed id: 9630226

Crystal structure of a tyrosine phosphorylated STAT-1 dimer bound to DNA.

X.Chen, U.Vinkemeier, Y.Zhao, D.Jeruzalmi, J.E.Darnell, J.Kuriyan.

ABSTRACT

The crystal structure of the DNA complex of a STAT-1 homodimer has been determined at 2.9 A resolution. STAT-1 utilizes a DNA-binding domain with an immunoglobulin fold, similar to that of NFkappaB and the p53 tumor suppressor protein. The STAT-1 dimer forms a contiguous C-shaped clamp around DNA that is stabilized by reciprocal and highly specific interactions between the SH2 domain of one monomer and the C-terminal segment, phosphorylated on tyrosine, of the other. The phosphotyrosine-binding site of the SH2 domain in each monomer is coupled structurally to the DNA-binding domain, suggesting a potential role for the SH2-phosphotyrosine interaction in the stabilization of DNA interacting elements.

Selected figure(s)

Figure 2.
Figure 2. Structure of the STAT-1 DNA Complex(A) Ribbon diagram of the STAT-1 core dimer on DNA. The component domains are colored green (coiled-coil domain), red (DNA-binding domain), orange (linker domain), cyan (SH2 domain). The tail segments are shown in magenta and yellow. Disordered loops (one in the coiled-coil domain and one connecting the SH2 domain to the tail segment) are shown as dotted lines. The phosphotyrosine residue is shown in a stick representation. The N and C termini of STAT-1 core are indicated by “N” and “C”. The DNA backbone is shown in gray. This and other ribbon diagrams were rendered using RIBBONS ([6]).(B) Molecular surface of the STAT-1 dimer in the same orientation as (A). The surface was calculated using GRASP ([31]) and rendered using RASTER3D ( [28]). The tail segments, shown in green and magenta, were not included in the surface generation. The surface is colored according to the local electrostatic potential, with blue and red representing positive and negative potential, respectively.

Figure 3.
Figure 3. Structure of the Coiled-Coil Domain of STAT-1The polypeptide backbone of the four helices is shown as a gray ribbon. The directions of the helices are indicated by arrows. All the side chains in the domain are depicted in the figure and are colored red (acidic), blue (basic), orange (polar), and yellow (hydrophobic). Note the clusters of acidic and basic residues on the surface. The only significant cluster of hydrophobic side chains on the surface corresponds to the site of attachment to the DNA-binding domain and is indicated by a dotted line.

The above figures are reprinted by permission from Cell Press: Cell (1998, 93, 827-839) copyright 1998.

Figures were selected by an automated process.