 |
PDBsum entry 2j8o
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Structural protein
|
PDB id
|
|
|
|
2j8o
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
|
|
|
|
|
|
Enzyme class:
|
|
E.C.2.7.11.1
- non-specific serine/threonine protein kinase.
|
|
|
|
|
|
|
Reaction:
|
|
|
1.
|
L-seryl-[protein] + ATP = O-phospho-L-seryl-[protein] + ADP + H+
|
|
2.
|
L-threonyl-[protein] + ATP = O-phospho-L-threonyl-[protein] + ADP + H+
|
|
|
|
|
|
|
L-seryl-[protein]
|
+
|
ATP
|
=
|
O-phospho-L-seryl-[protein]
|
+
|
ADP
|
+
|
H(+)
|
|
|
|
|
|
|
L-threonyl-[protein]
|
+
|
ATP
|
=
|
O-phospho-L-threonyl-[protein]
|
+
|
ADP
|
+
|
H(+)
|
|
|
|
|
|
|
|
|
|
|
|
|
Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
| |
|
|
| |
|
DOI no:
|
J Mol Biol
371:469-480
(2007)
|
|
PubMed id:
|
|
|
|
|
|
| |
|
Rigid conformation of an immunoglobulin domain tandem repeat in the A-band of the elastic muscle protein titin.
|
|
S.Müller,
S.Lange,
M.Gautel,
M.Wilmanns.
|
|
|
|
|
| |
ABSTRACT
|
|
|
|
| |
|
|
Most of the structure of the giant muscle protein titin is formed by small
modular domains. Many of them are predicted to be arranged in repeats with short
linkers that may be key determinants of the peculiar elastic properties of
titin. Here, we present the molecular structure of a tandem arrangement of two
immunoglobulin-like domains, A168 and A169, located within the A-band segment of
titin. The two domains are connected by a 17 residue long beta-strand and form a
common interface. Based on these data, we establish general principles to
estimate the amount of conformational flexibility of tandem domain motifs in
titin. An unusual bulge within the second domain, A169, is directly involved
into binding to a sarcomeric ligand, MURF-1, thus suggesting a dual role of this
tandem for both the mechanical properties of titin and for sarcomeric signaling.
|
|
|
|
|
|
| |
Selected figure(s)
|
|
|
|
| |
|
|
|
|
|
|
Figure 2.
Figure 2. Schematic presentation of the A168–A169
connecting β-strand (blue) and interacting β-strands from IG
β-sheets. The β-strand residues are colored according to the
scheme used in Figure 6, highlighting whether they belong to the
first or the second I-set IG β-sheet. The background colors of
each β-sheet are adopted from the scheme used in Figure 1,
indicating whether the β-sheet belongs to domain A168 or A169.
Residue numbers are given for the first and last residue of each
β-strand. The β-strand labels are indicated in appropriate
colors above and below the presentation.
|
|
Figure 7.
Figure 7. Model of the domain architecture and ligand
interaction sites from the titin A-band/M-band transition zone.
IG domain tandems, red/dark red; FN-III domains, light brown;
titin kinase, cyan; the interaction sites for several A-band and
kinase downstream ligands^15 are shown schematically, except for
the PB1 domain of NBR1 (green) with an available molecular
structure.^51 The domain nomenclature is indicated on top.
|
|
|
|
|
|
| |
The above figures are
reprinted
by permission from Elsevier:
J Mol Biol
(2007,
371,
469-480)
copyright 2007.
|
|
| |
Figures were
selected
by an automated process.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
|
Literature references that cite this PDB file's key reference
|
|
|
| |
PubMed id
|
|
Reference
|
|
|
|
|
|
J.Hsin,
J.Strümpfer,
E.H.Lee,
and
K.Schulten
(2011).
Molecular origin of the hierarchical elasticity of titin: simulation, experiment, and theory.
|
| |
Annu Rev Biophys,
40,
187-203.
|
|
|
|
|
|
|
L.Tskhovrebova,
and
J.Trinick
(2010).
Roles of titin in the structure and elasticity of the sarcomere.
|
| |
J Biomed Biotechnol,
2010,
612482.
|
|
|
|
|
|
|
A.Kontrogianni-Konstantopoulos,
M.A.Ackermann,
A.L.Bowman,
S.V.Yap,
and
R.J.Bloch
(2009).
Muscle giants: molecular scaffolds in sarcomerogenesis.
|
| |
Physiol Rev,
89,
1217-1267.
|
|
|
|
|
|
|
C.A.Otey,
R.Dixon,
C.Stack,
and
S.M.Goicoechea
(2009).
Cytoplasmic Ig-domain proteins: cytoskeletal regulators with a role in human disease.
|
| |
Cell Motil Cytoskeleton,
66,
618-634.
|
|
|
|
|
|
|
E.von Castelmur,
M.Marino,
D.I.Svergun,
L.Kreplak,
Z.Ucurum-Fotiadis,
P.V.Konarev,
A.Urzhumtsev,
D.Labeit,
S.Labeit,
and
O.Mayans
(2008).
A regular pattern of Ig super-motifs defines segmental flexibility as the elastic mechanism of the titin chain.
|
| |
Proc Natl Acad Sci U S A,
105,
1186-1191.
|
|
|
PDB codes:
|
|
|
|
|
|
|
|
M.V.Razumova,
K.L.Bezold,
A.Y.Tu,
M.Regnier,
and
S.P.Harris
(2008).
Contribution of the myosin binding protein C motif to functional effects in permeabilized rat trabeculae.
|
| |
J Gen Physiol,
132,
575-585.
|
|
|
|
|
|
|
N.Pinotsis,
S.Lange,
J.C.Perriard,
D.I.Svergun,
and
M.Wilmanns
(2008).
Molecular basis of the C-terminal tail-to-tail assembly of the sarcomeric filament protein myomesin.
|
| |
EMBO J,
27,
253-264.
|
|
|
PDB code:
|
|
|
|
|
|
|
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
codes are
shown on the right.
|
|
Links
