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PDBsum entry 1bf5
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Gene regulation/DNA
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PDB id
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1bf5
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Crystal structure of a tyrosine phosphorylated stat-1 dimer bound to DNA.
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Authors
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X.Chen,
U.Vinkemeier,
Y.Zhao,
D.Jeruzalmi,
J.E.Darnell,
J.Kuriyan.
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Ref.
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Cell, 1998,
93,
827-839.
[DOI no: ]
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PubMed id
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Abstract
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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.
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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.
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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.
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The above figures are
reprinted
by permission from Cell Press:
Cell
(1998,
93,
827-839)
copyright 1998.
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