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PDBsum entry 1yxq
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Contractile protein
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PDB id
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1yxq
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DOI no:
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Chem Biol
12:287-291
(2005)
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PubMed id:
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Structural basis of swinholide A binding to actin.
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V.A.Klenchin,
R.King,
J.Tanaka,
G.Marriott,
I.Rayment.
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ABSTRACT
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Marine toxins targeting the actin cytoskeleton represent a new and promising
class of anti-cancer compounds. Here we present a 2.0 A resolution structure of
swinholide A, a marine macrolide, bound to two actin molecules. The structure
demonstrates that the actin dimer in the complex does not represent a
physiologically relevant entity, for the two actin molecules do not interact
with each other. The swinholide A actin binding site is the same as that
targeted by toxins of the trisoxazole family and numerous actin binding
proteins, highlighting the importance of this site in actin polymerization. The
observed structure reveals the mechanism of action of swinholide A and provides
a structural framework about which to design new agents directed at the
cytoskeleton.
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Selected figure(s)
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Figure 1.
Figure 1. Structure, Electron Density, and Ligand Contacts
for the Actin-Swinholide A Complex
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Figure 2.
Figure 2. Swinholide A and Kabiramide C Occupy the Same
Binding Site on Actin
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The above figures are
reprinted
by permission from Cell Press:
Chem Biol
(2005,
12,
287-291)
copyright 2005.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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J.C.Blain,
Y.F.Mok,
J.Kubanek,
and
J.S.Allingham
(2010).
Two molecules of lobophorolide cooperate to stabilize an actin dimer using both their "ring" and "tail" region.
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Chem Biol,
17,
802-807.
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PDB code:
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M.R.Sawaya,
D.S.Kudryashov,
I.Pashkov,
H.Adisetiyo,
E.Reisler,
and
T.O.Yeates
(2008).
Multiple crystal structures of actin dimers and their implications for interactions in the actin filament.
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Acta Crystallogr D Biol Crystallogr,
64,
454-465.
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PDB codes:
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S.Mouilleron,
S.Guettler,
C.A.Langer,
R.Treisman,
and
N.Q.McDonald
(2008).
Molecular basis for G-actin binding to RPEL motifs from the serum response factor coactivator MAL.
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EMBO J,
27,
3198-3208.
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PDB codes:
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J.L.Melville,
I.H.Moal,
C.Baker-Glenn,
P.E.Shaw,
G.Pattenden,
and
J.D.Hirst
(2007).
The structural determinants of macrolide-actin binding: in silico insights.
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Biophys J,
92,
3862-3867.
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J.W.Blunt,
B.R.Copp,
W.P.Hu,
M.H.Munro,
P.T.Northcote,
and
M.R.Prinsep
(2007).
Marine natural products.
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Nat Prod Rep,
24,
31-86.
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M.Böhl,
S.Tietze,
A.Sokoll,
S.Madathil,
F.Pfennig,
J.Apostolakis,
K.Fahmy,
and
H.O.Gutzeit
(2007).
Flavonoids affect actin functions in cytoplasm and nucleus.
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Biophys J,
93,
2767-2780.
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D.S.Kudryashov,
M.R.Sawaya,
H.Adisetiyo,
T.Norcross,
G.Hegyi,
E.Reisler,
and
T.O.Yeates
(2005).
The crystal structure of a cross-linked actin dimer suggests a detailed molecular interface in F-actin.
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Proc Natl Acad Sci U S A,
102,
13105-13110.
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PDB code:
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J.S.Allingham,
A.Zampella,
M.V.D'Auria,
and
I.Rayment
(2005).
Structures of microfilament destabilizing toxins bound to actin provide insight into toxin design and activity.
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Proc Natl Acad Sci U S A,
102,
14527-14532.
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PDB codes:
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
code is
shown on the right.
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Links
