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PDBsum entry 1io0
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Protein binding
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PDB id
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1io0
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Contents |
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* Residue conservation analysis
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Biophys J
83:2716-2725
(2002)
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PubMed id:
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Crystal structure of the C-terminal half of tropomodulin and structural basis of actin filament pointed-end capping.
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I.Krieger,
A.Kostyukova,
A.Yamashita,
Y.Nitanai,
Y.Maéda.
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ABSTRACT
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Tropomodulin is the unique pointed-end capping protein of the actin-tropomyosin
filament. By blocking elongation and depolymerization, tropomodulin regulates
the architecture and the dynamics of the filament. Here we report the crystal
structure at 1.45-A resolution of the C-terminal half of tropomodulin (C20), the
actin-binding moiety of tropomodulin. C20 is a leucine-rich repeat domain, and
this is the first actin-associated protein with a leucine-rich repeat. Binding
assays suggested that C20 also interacts with the N-terminal fragment, M1-M2-M3,
of nebulin. Based on the crystal structure, we propose a model for C20 docking
to the actin subunit at the pointed end. Although speculative, the model is
consistent with the idea that a tropomodulin molecule competes with an actin
subunit for a pointed end. The model also suggests that interactions with
tropomyosin, actin, and nebulin are all possible sources of influences on the
dynamic properties of pointed-end capping by tropomodulin.
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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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C.T.Pappas,
K.T.Bliss,
A.Zieseniss,
and
C.C.Gregorio
(2011).
The Nebulin family: an actin support group.
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Trends Cell Biol,
21,
29-37.
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A.Skwarek-Maruszewska,
M.Boczkowska,
A.L.Zajac,
E.Kremneva,
T.Svitkina,
R.Dominguez,
and
P.Lappalainen
(2010).
Different localizations and cellular behaviors of leiomodin and tropomodulin in mature cardiomyocyte sarcomeres.
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Mol Biol Cell,
21,
3352-3361.
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B.Qualmann,
and
M.M.Kessels
(2009).
New players in actin polymerization--WH2-domain-containing actin nucleators.
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Trends Cell Biol,
19,
276-285.
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K.L.Hindle,
J.Bella,
and
S.C.Lovell
(2009).
Quantitative analysis and prediction of curvature in leucine-rich repeat proteins.
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Proteins,
77,
342-358.
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R.Dominguez
(2009).
Actin filament nucleation and elongation factors--structure-function relationships.
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Crit Rev Biochem Mol Biol,
44,
351-366.
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D.Chereau,
M.Boczkowska,
A.Skwarek-Maruszewska,
I.Fujiwara,
D.B.Hayes,
G.Rebowski,
P.Lappalainen,
T.D.Pollard,
and
R.Dominguez
(2008).
Leiomodin is an actin filament nucleator in muscle cells.
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Science,
320,
239-243.
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N.Matsushima,
T.Tanaka,
P.Enkhbayar,
T.Mikami,
M.Taga,
K.Yamada,
and
Y.Kuroki
(2007).
Comparative sequence analysis of leucine-rich repeats (LRRs) within vertebrate toll-like receptors.
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BMC Genomics,
8,
124.
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H.Gong,
V.Hatch,
L.Ali,
W.Lehman,
R.Craig,
and
L.S.Tobacman
(2005).
Mini-thin filaments regulated by troponin-tropomyosin.
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Proc Natl Acad Sci U S A,
102,
656-661.
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N.J.Greenfield,
A.S.Kostyukova,
and
S.E.Hitchcock-DeGregori
(2005).
Structure and tropomyosin binding properties of the N-terminal capping domain of tropomodulin 1.
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Biophys J,
88,
372-383.
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E.Ehler,
V.M.Fowler,
and
J.C.Perriard
(2004).
Myofibrillogenesis in the developing chicken heart: role of actin isoforms and of the pointed end actin capping protein tropomodulin during thin filament assembly.
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Dev Dyn,
229,
745-755.
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P.Enkhbayar,
M.Kamiya,
M.Osaki,
T.Matsumoto,
and
N.Matsushima
(2004).
Structural principles of leucine-rich repeat (LRR) proteins.
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Proteins,
54,
394-403.
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S.Lu,
J.Symersky,
S.Li,
M.Carson,
L.Chen,
E.Meehan,
and
M.Luo
(2004).
Structural genomics of Caenorhabditis elegans: crystal structure of the tropomodulin C-terminal domain.
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Proteins,
56,
384-386.
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PDB code:
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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
