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PDBsum entry 1wlh
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Structural protein
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PDB id
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1wlh
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References listed in PDB file
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Key reference
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Title
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Molecular structure of the rod domain of dictyostelium filamin.
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Authors
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G.M.Popowicz,
R.Müller,
A.A.Noegel,
M.Schleicher,
R.Huber,
T.A.Holak.
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Ref.
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J Mol Biol, 2004,
342,
1637-1646.
[DOI no: ]
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PubMed id
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Abstract
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Dictyostelium discoideum filamin (ddFLN) is a two-chain F-actin crosslinking
protein with an N-terminal actin-binding domain and a rod domain constructed
from six tandem repeats of a 100 residue motif that has an immunoglobulin (Ig)
fold. We report the 2.8 A resolution crystal structure of a homodimer of rod
repeats 4, 5 and 6. The two chains are arranged in an antiparallel fashion and
form an elongated element, which is shortened, however, compared to a fully
extended, linear configuration because the long axis of each Ig domain is
arranged at an angle to the long axis of the rod. Same arrangement of repeats
should also be present in the rod domain of human FLNa, much longer than
Dictyostelium FLN, which forms an extended structure able to crosslink F-actin
chains over distances of more than 1000 A.
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Figure 2.
Figure 2. Interpreted electron density map of the border
region between repeats 4 and 5. Pro647 placed between two
b-strands connects repeats. Additionally, side-chains of Glu565
and Arg734 form a salt-bridge.
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Figure 4.
Figure 4. A homodimer model of the whole ddFLN protein.
Inter-repeat angles are taken from repeats 4 and 5. Rod domain
builds an extended chain interconnecting two actin-binding
domains.
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The above figures are
reprinted
by permission from Elsevier:
J Mol Biol
(2004,
342,
1637-1646)
copyright 2004.
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