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PDBsum entry 1blq

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Calcium-binding protein PDB id
1blq
Jmol
Contents
Protein chain
90 a.a. *
* Residue conservation analysis
PDB id:
1blq
Name: Calcium-binding protein
Title: Structure and interaction site of the regulatory domain of troponin-c when complexed with the 96-148 region of troponin-i, nmr, 29 structures
Structure: N-troponin c. Chain: a. Fragment: regulatory. Synonym: sntnc. Engineered: yes. Other_details: complex of sntnc with tni peptide
Source: Gallus gallus. Chicken. Organism_taxid: 9031. Cell_line: bl21. Organ: skeletal. Tissue: skeletal muscle. Expressed in: escherichia coli. Expression_system_taxid: 562.
NMR struc: 29 models
Authors: R.T.Mckay,J.R.Pearlstone,D.C.Corson,S.M.Gagne,L.B.Smillie, B.D.Sykes
Key ref:
R.T.McKay et al. (1998). Structure and interaction site of the regulatory domain of troponin-C when complexed with the 96-148 region of troponin-I. Biochemistry, 37, 12419-12430. PubMed id: 9730814 DOI: 10.1021/bi9809019
Date:
19-Jul-98     Release date:   13-Jan-99    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P02588  (TNNC2_CHICK) -  Troponin C, skeletal muscle
Seq:
Struc:
163 a.a.
90 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Biochemical function     calcium ion binding     1 term  

 

 
DOI no: 10.1021/bi9809019 Biochemistry 37:12419-12430 (1998)
PubMed id: 9730814  
 
 
Structure and interaction site of the regulatory domain of troponin-C when complexed with the 96-148 region of troponin-I.
R.T.McKay, J.R.Pearlstone, D.C.Corson, S.M.Gagné, L.B.Smillie, B.D.Sykes.
 
  ABSTRACT  
 
The structure of the regulatory domain of chicken skeletal troponin-C (residues 1-90) when complexed with the major inhibitory region (residues 96-148) of chicken skeletal troponin-I was determined using multinuclear, multidimensional NMR spectroscopy. This complex represents the first interaction formed between the regulatory domain of troponin-C and troponin-I after calcium binding in the regulation of muscle contraction. The stoichiometry of the complex was determined to be 1:1, with a dissociation constant in the 1-40 microM range. The structure of troponin-C in the complex was calculated from 1039 NMR distance and 111 dihedral angle restraints. When compared to the structure of this domain in the calcium saturated "open" form but in the absence of troponin-I, the bound structure appears to be slightly more "closed". The troponin-I peptide-binding site was found to be in the hydrophobic pocket of calcium saturated troponin-C, using edited/filtered NMR experiments and chemical shift mapping of changes induced in the regulatory domain upon peptide binding. The troponin-I peptide (residues 96-148) was found to bind to the regulatory domain of troponin-C very similarly, but not identically, to a shorter troponin-I peptide (region 115-131) thought to represent the major interaction site of troponin-I for this domain of troponin-C.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19483081 T.Kobayashi, S.E.Patrick, and M.Kobayashi (2009).
Ala scanning of the inhibitory region of cardiac troponin I.
  J Biol Chem, 284, 20052-20060.  
18162171 M.X.Li, I.M.Robertson, and B.D.Sykes (2008).
Interaction of cardiac troponin with cardiotonic drugs: a structural perspective.
  Biochem Biophys Res Commun, 369, 88-99.  
16432210 M.Ikura, and J.B.Ames (2006).
Genetic polymorphism and protein conformational plasticity in the calmodulin superfamily: two ways to promote multifunctionality.
  Proc Natl Acad Sci U S A, 103, 1159-1164.  
16531415 T.Kobayashi, and R.J.Solaro (2006).
Increased Ca2+ affinity of cardiac thin filaments reconstituted with cardiomyopathy-related mutant cardiac troponin I.
  J Biol Chem, 281, 13471-13477.  
15670158 A.O.Tiroli, L.Tasic, C.L.Oliveira, C.Bloch, I.Torriani, C.S.Farah, and C.H.Ramos (2005).
Mapping contacts between regulatory domains of skeletal muscle TnC and TnI by analyses of single-chain chimeras.
  FEBS J, 272, 779-790.  
12732641 D.A.Lindhout, and B.D.Sykes (2003).
Structure and dynamics of the C-domain of human cardiac troponin C in complex with the inhibitory region of human cardiac troponin I.
  J Biol Chem, 278, 27024-27034.
PDB code: 1ozs
12524267 F.Pitici (2003).
Structural preference for changes in the direction of the Ca2+-induced transition: a study of the regulatory domain of skeletal troponin-C.
  Biophys J, 84, 82.  
12909617 W.J.Dong, J.M.Robinson, J.Xing, and H.C.Cheung (2003).
Kinetics of conformational transitions in cardiac troponin induced by Ca2+ dissociation determined by Förster resonance energy transfer.
  J Biol Chem, 278, 42394-42402.  
12846843 Y.M.Liou, and M.W.Chen (2003).
Calcium-dependent protein-protein interactions induce changes in proximity relationships of Cys48 and Cys64 in chicken skeletal troponin I.
  Eur J Biochem, 270, 3092-3100.  
12207022 D.G.Ward, M.P.Cornes, and I.P.Trayer (2002).
Structural consequences of cardiac troponin I phosphorylation.
  J Biol Chem, 277, 41795-41801.  
12060657 X.Wang, M.X.Li, and B.D.Sykes (2002).
Structure of the regulatory N-domain of human cardiac troponin C in complex with human cardiac troponin I147-163 and bepridil.
  J Biol Chem, 277, 31124-31133.
PDB code: 1lxf
11391787 J.Song, and J.L.Markley (2001).
NMR chemical shift mapping of the binding site of a protein proteinase inhibitor: changes in the (1)H, (13)C and (15)N NMR chemical shifts of turkey ovomucoid third domain upon binding to bovine chymotrypsin A(alpha).
  J Mol Recognit, 14, 166-171.  
11567104 X.J.Morelli, P.N.Palma, F.Guerlesquin, and A.C.Rigby (2001).
A novel approach for assessing macromolecular complexes combining soft-docking calculations with NMR data.
  Protein Sci, 10, 2131-2137.  
11423417 Z.Li, J.Gergely, and T.Tao (2001).
Proximity relationships between residue 117 of rabbit skeletal troponin-I and residues in troponin-C and actin.
  Biophys J, 81, 321-333.  
  10933496 C.S.Tung, M.E.Wall, S.C.Gallagher, and J.Trewhella (2000).
A model of troponin-I in complex with troponin-C using hybrid experimental data: the inhibitory region is a beta-hairpin.
  Protein Sci, 9, 1312-1326.
PDB code: 1ew7
10913289 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.
  Biochemistry, 39, 8782-8790.  
10715110 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.
  Biochemistry, 39, 2902-2911.  
10819994 R.A.Atkinson, C.Joseph, F.Dal Piaz, L.Birolo, G.Stier, P.Pucci, and A.Pastore (2000).
Binding of alpha-actinin to titin: implications for Z-disk assembly.
  Biochemistry, 39, 5255-5264.  
11027154 R.T.McKay, L.F.Saltibus, M.X.Li, and B.D.Sykes (2000).
Energetics of the induced structural change in a Ca2+ regulatory protein: Ca2+ and troponin I peptide binding to the E41A mutant of the N-domain of skeletal troponin C.
  Biochemistry, 39, 12731-12738.  
11112516 Y.Luo, J.Leszyk, B.Li, J.Gergely, and T.Tao (2000).
Proximity relationships between residue 6 of troponin I and residues in troponin C: further evidence for extended conformation of troponin C in the troponin complex.
  Biochemistry, 39, 15306-15315.  
10373418 C.H.Ramos (1999).
Mapping subdomains in the C-terminal region of troponin I involved in its binding to troponin C and to thin filament.
  J Biol Chem, 274, 18189-18195.  
10506219 D.Szczesna, R.Zhang, J.Zhao, M.Jones, and J.D.Potter (1999).
The role of the NH(2)- and COOH-terminal domains of the inhibitory region of troponin I in the regulation of skeletal muscle contraction.
  J Biol Chem, 274, 29536-29542.  
9876151 L.Smith, N.J.Greenfield, and S.E.Hitchcock-DeGregori (1999).
Mutations in the N- and D-helices of the N-domain of troponin C affect the C-domain and regulatory function.
  Biophys J, 76, 400-408.  
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.