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PDBsum entry 1v05
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Actin-binding protein
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PDB id
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1v05
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References listed in PDB file
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Key reference
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Title
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Structural basis for vertebrate filamin dimerization.
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Authors
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R.Pudas,
T.R.Kiema,
P.J.Butler,
M.Stewart,
J.Ylänne.
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Ref.
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Structure, 2005,
13,
111-119.
[DOI no: ]
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PubMed id
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Abstract
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Filamins are essential in cell motility and many developmental processes. They
are large actin cross linking proteins that contain actin binding domains in
their N termini and a long rod region constructed from 24 tandem Ig domains.
Dimerization is crucial for the actin crosslinking function of filamins and
requires the most C-terminal Ig domain. We describe here the crystal structure
of this 24th Ig domain (Ig24) of human filamin C and show how it mediates
dimerization. The dimer interface is novel and quite different to that seen in
the Dictyostelium discoideum filamin analog. The sequence signature of the
dimerization interface suggests that the C-terminal domains of all vertebrate
filamins share the same dimerization mechanism. Furthermore, we show that point
mutations in the dimerization interface disrupt the dimer and that the
dissociation constant for recombinant Ig24 is in the micromolar range.
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Figure 4.
Figure 4. Filamin Domain 24 Dimerization Interface
(A)
The hydrophobic stacking of strand C in the dimer interface.
Side chains of Met2669 pack against Gly2671 of the neighboring
monomer, creating hydrophobic interactions.
(B) Hydrogen
bonding between the monomers at strand D.
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The above figure is
reprinted
by permission from Cell Press:
Structure
(2005,
13,
111-119)
copyright 2005.
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