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PDBsum entry 2nqc
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Immune system
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PDB id
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2nqc
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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 human filamin c domain 23 and small angle scattering model for filamin c 23-24 dimer.
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Authors
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L.Sjekloća,
R.Pudas,
B.Sjöblom,
P.Konarev,
O.Carugo,
V.Rybin,
T.R.Kiema,
D.Svergun,
J.Ylänne,
K.D.Carugo.
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Ref.
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J Mol Biol, 2007,
368,
1011-1023.
[DOI no: ]
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PubMed id
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Abstract
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Filamin C is a dimeric, actin-binding protein involved in organization of
cortical cytoskeleton and of the sarcomere. We performed crystallographic,
small-angle X-ray scattering and analytical ultracentrifugation experiments on
the constructs containing carboxy-terminal domains of the protein (domains 23-24
and 19-21). The crystal structure of domain 23 of filamin C showed that the
protein adopts the expected immunoglobulin (Ig)-like fold. Small-angle X-ray
scattering experiments performed on filamin C tandem Ig-like domains 23 and 24
reveal a dimer that is formed by domain 24 and that domain 23 has little
interactions with itself or with domain 24, while the analytical
ultracentrifugation experiments showed that the filamin C domains 19-21 form
elongated monomers in diluted solutions.
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Figure 1.
Figure 1. Cartoon representation in stereo of Ig-like domain
23 from filamin C. β-Strand elements are represented in yellow,
helical turns in red, and the connecting loops are coloured in
green.
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Figure 4.
Figure 4. (a) Experimental X-ray scattering pattern from
filamin C Ig-like domains 23–24 dimer. Scattering from a
typical ab initio model computed by DAMMIN (continuous line,
red) and from the three-dimensional model with added linker
parts between domains 23 and 24 obtained by BUNCH^8 (broken
line, blue). The plot displays the logarithm of the scattering
intensity as a function of momentum transfer s = 4π sin(θ)/λ,
where 2θ is the scattering angle and λ = 0.15 nm is the X-ray
wavelength. The distance distribution function is displayed in
the inner window on top right. (b) Ab initio and rigid models of
the filamin C Ig-like domains 23–24 dimer. Ab initio models of
filamin C Ig-like domain 23–24 dimer superimposed with the
rigid body models. The ab initio models obtained by DAMMIN are
displayed as gray semitransparent spheres, the models obtained
by BUNCH as C^α traces (the two monomers are coloured red and
blue, the linkers are green). Top panel, models without
symmetry; bottom panel, models with P2 symmetry axis (vertical
axis on the bottom left). The right view is rotated clockwise
around the horizontal axis. The bar represents the length of 50
Å and is shown at the top left.
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The above figures are
reprinted
by permission from Elsevier:
J Mol Biol
(2007,
368,
1011-1023)
copyright 2007.
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