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PDBsum entry 1vfq
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Protein binding
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PDB id
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1vfq
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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 coactosin-Like protein at 1.9 a resolution.
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Authors
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X.Li,
X.Liu,
Z.Lou,
X.Duan,
H.Wu,
Y.Liu,
Z.Rao.
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Ref.
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Protein Sci, 2004,
13,
2845-2851.
[DOI no: ]
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PubMed id
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Abstract
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Human coactosin-like protein (CLP) shares high homology with coactosin, a
filamentous (F)-actin binding protein, and interacts with 5LO and F-actin. As a
tumor antigen, CLP is overexpressed in tumor tissue cells or cell lines, and the
encoded epitopes can be recognized by cellular and humoral immune systems. To
gain a better understanding of its various functions and interactions with
related proteins, the crystal structure of CLP expressed in Escherichia coli has
been determined to 1.9 A resolution. The structure features a central beta-sheet
surrounded by helices, with two very tight hydrophobic cores on each side of the
sheet. CLP belongs to the actin depolymerizing protein superfamily, and is
similar to yeast cofilin and actophilin. Based on our structural analysis, we
observed that CLP forms a polymer along the crystallographic b axis with the
exact same repeat distance as F-actin. A model for the CLP polymer and F-actin
binding has therefore been proposed.
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Figure 3.
Figure 3. Comparison of CLP structure with actophorin and
yeast cofilin. (A) Stereo view of CLP (red) superimposed with
cofilin (yellow) and actophorin (purple). The figure was
prepared with MOLSCRIPT. (B) Comparison of the CLP molecular
surface charge distribution with those of cofilin and
actophorin. The positive charges are shown in the first row; the
negative, which is the opposite sides of the positive, are shown
in the second row. The surface of CLP is more positively charged
in the N-terminal and  4- 5 loop
regions. This figure was prepared with SPDBV (Guex and Peitsch
1997).
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Figure 5.
Figure 5. A model for CLP polymer binding with F-actin and
other proteins. (A) CLP polymer and F-actin have the same
repeating distance. The morphologies of the two polymers match
each other very well. Its long flexible C-terminal arm may help
CLP binding other molecules. (B) A model for CLP polymer binding
with F-actin. (C) CLP-F-actin copolymer binding with other
proteins (red). The F-actin diagram is provided by Amy McGough
(Baylor College of Medicine, Houston, TX). The models in B and C
were prepared with Photoshop, and the charged surface model and
the CPK (red) model were prepared with SPDBV and MOLSCRIPT,
respectively.
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The above figures are
reprinted
by permission from the Protein Society:
Protein Sci
(2004,
13,
2845-2851)
copyright 2004.
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