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PDBsum entry 1fi5
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Contractile protein
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PDB id
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1fi5
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Contents |
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* Residue conservation analysis
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PDB id:
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Contractile protein
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Title:
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Nmr structure of thE C terminal domain of cardiac troponin c bound to the n terminal domain of cardiac troponin i.
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Structure:
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Protein (troponin c). Chain: a. Fragment: residues 81 - 161. Engineered: yes
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Source:
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Gallus gallus. Chicken. Organism_taxid: 9031. Organ: heart. Tissue: muscle. Cell: myocyte. Cellular_location: thin filament. Expressed in: escherichia coli bl21(de3). Expression_system_taxid: 469008.
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NMR struc:
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20 models
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Authors:
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G.M.Gasmi-Seabrook,J.W.Howarth,N.Finley,E.Abusamhadneh,V.Gaponenko, R.M.Brito,R.J.Solaro,P.R.Rosevear
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Key ref:
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G.M.Gasmi-Seabrook
et al.
(1999).
Solution structures of the C-terminal domain of cardiac troponin C free and bound to the N-terminal domain of cardiac troponin I.
Biochemistry,
38,
8313-8322.
PubMed id:
DOI:
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Date:
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03-Aug-00
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Release date:
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23-Aug-00
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Supersedes:
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PROCHECK
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Headers
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References
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P09860
(TNNC1_CHICK) -
Troponin C, slow skeletal and cardiac muscles from Gallus gallus
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Seq: Struc:
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161 a.a.
81 a.a.
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Key: |
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PfamA domain |
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Secondary structure |
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CATH domain |
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DOI no:
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Biochemistry
38:8313-8322
(1999)
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PubMed id:
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Solution structures of the C-terminal domain of cardiac troponin C free and bound to the N-terminal domain of cardiac troponin I.
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G.M.Gasmi-Seabrook,
J.W.Howarth,
N.Finley,
E.Abusamhadneh,
V.Gaponenko,
R.M.Brito,
R.J.Solaro,
P.R.Rosevear.
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ABSTRACT
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The N-terminal domain of cardiac troponin I (cTnI) comprising residues 33-80 and
lacking the cardiac-specific amino terminus forms a stable binary complex with
the C-terminal domain of cardiac troponin C (cTnC) comprising residues 81-161.
We have utilized heteronuclear multidimensional NMR to assign the backbone and
side-chain resonances of Ca2+-saturated cTnC(81-161) both free and bound to
cTnI(33-80). No significant differences were observed between secondary
structural elements determined for free and cTnI(33-80)-bound cTnC(81-161). We
have determined solution structures of Ca2+-saturated cTnC(81-161) free and
bound to cTnI(33-80). While the tertiary structure of cTnC(81-161) is
qualitatively similar to that observed free in solution, the binding of
cTnI(33-80) results mainly in an opening of the structure and movement of the
loop region between helices F and G. Together, these movements provide the
binding site for the N-terminal domain of cTnI. The putative binding site for
cTnI(33-80) was determined by mapping amide proton and nitrogen chemical shift
changes, induced by the binding of cTnI(33-80), onto the C-terminal cTnC
structure. The binding interface for cTnI(33-80), as suggested from chemical
shift changes, involves predominantly hydrophobic interactions located in the
expanded hydrophobic pocket. The largest chemical shift changes were observed in
the loop region connecting helices F and G. Inspection of available TnC
sequences reveals that these residues are highly conserved, suggesting a common
binding motif for the Ca2+/Mg2+-dependent interaction site in the TnC/TnI
complex.
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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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I.M.Robertson,
M.X.Li,
and
B.D.Sykes
(2009).
Solution structure of human cardiac troponin C in complex with the green tea polyphenol, (-)-epigallocatechin 3-gallate.
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J Biol Chem,
284,
23012-23023.
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PDB code:
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M.X.Li,
I.M.Robertson,
and
B.D.Sykes
(2008).
Interaction of cardiac troponin with cardiotonic drugs: a structural perspective.
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Biochem Biophys Res Commun,
369,
88-99.
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P.L.Engel,
T.Kobayashi,
B.Biesiadecki,
J.Davis,
S.Tikunova,
S.Wu,
and
R.J.Solaro
(2007).
Identification of a region of troponin I important in signaling cross-bridge-dependent activation of cardiac myofilaments.
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J Biol Chem,
282,
183-193.
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H.Chen,
and
H.X.Zhou
(2005).
Prediction of interface residues in protein-protein complexes by a consensus neural network method: test against NMR data.
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Proteins,
61,
21-35.
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M.X.Li,
X.Wang,
and
B.D.Sykes
(2004).
Structural based insights into the role of troponin in cardiac muscle pathophysiology.
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J Muscle Res Cell Motil,
25,
559-579.
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N.L.Finley,
and
P.R.Rosevear
(2004).
Introduction of negative charge mimicking protein kinase C phosphorylation of cardiac troponin I. Effects on cardiac troponin C.
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J Biol Chem,
279,
54833-54840.
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S.Takeda,
A.Yamashita,
K.Maeda,
and
Y.Maéda
(2003).
Structure of the core domain of human cardiac troponin in the Ca(2+)-saturated form.
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Nature,
424,
35-41.
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PDB codes:
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A.Dvoretsky,
E.M.Abusamhadneh,
J.W.Howarth,
and
P.R.Rosevear
(2002).
Solution structure of calcium-saturated cardiac troponin C bound to cardiac troponin I.
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J Biol Chem,
277,
38565-38570.
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PDB code:
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D.G.Ward,
M.P.Cornes,
and
I.P.Trayer
(2002).
Structural consequences of cardiac troponin I phosphorylation.
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J Biol Chem,
277,
41795-41801.
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M.B.Abbott,
W.J.Dong,
A.Dvoretsky,
B.DaGue,
R.M.Caprioli,
H.C.Cheung,
and
P.R.Rosevear
(2001).
Modulation of cardiac troponin C-cardiac troponin I regulatory interactions by the amino-terminus of cardiac troponin I.
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Biochemistry,
40,
5992-6001.
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M.X.Li,
L.Spyracopoulos,
N.Beier,
J.A.Putkey,
and
B.D.Sykes
(2000).
Interaction of cardiac troponin C with Ca(2+) sensitizer EMD 57033 and cardiac troponin I inhibitory peptide.
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Biochemistry,
39,
8782-8790.
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P.Mercier,
M.X.Li,
and
B.D.Sykes
(2000).
Role of the structural domain of troponin C in muscle regulation: NMR studies of Ca2+ binding and subsequent interactions with regions 1-40 and 96-115 of troponin I.
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Biochemistry,
39,
2902-2911.
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Y.Li,
M.L.Love,
J.A.Putkey,
and
C.Cohen
(2000).
Bepridil opens the regulatory N-terminal lobe of cardiac troponin C.
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Proc Natl Acad Sci U S A,
97,
5140-5145.
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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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}
}
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