PDBsum entry 1jc2

Go to PDB code: 
protein metals links
Structural protein PDB id
Protein chain
75 a.a. *
_CA ×2
* Residue conservation analysis
PDB id:
Name: Structural protein
Title: Complex of thE C-domain of troponin c with residues 1-40 of troponin i
Structure: Troponin c, skeletal muscle. Chain: a. Fragment: residues 89-163 of gb entry 212778. Engineered: yes
Source: Gallus gallus. Chicken. Organism_taxid: 9031. Gene: stnc. Expressed in: escherichia coli. Expression_system_taxid: 562.
NMR struc: 30 models
Authors: P.Mercier,L.Spyracopoulos,B.D.Sykes
Key ref:
P.Mercier et al. (2001). Structure, dynamics, and thermodynamics of the structural domain of troponin C in complex with the regulatory peptide 1-40 of troponin I. Biochemistry, 40, 10063-10077. PubMed id: 11513585 DOI: 10.1021/bi010748+
07-Jun-01     Release date:   14-Sep-01    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P02588  (TNNC2_CHICK) -  Troponin C, skeletal muscle
163 a.a.
75 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 1 residue position (black cross)

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


DOI no: 10.1021/bi010748+ Biochemistry 40:10063-10077 (2001)
PubMed id: 11513585  
Structure, dynamics, and thermodynamics of the structural domain of troponin C in complex with the regulatory peptide 1-40 of troponin I.
P.Mercier, L.Spyracopoulos, B.D.Sykes.
The structure of the calcium-saturated C-domain of skeletal troponin C (CTnC) in complex with a regulatory peptide comprising residues 1-40 (Rp40) of troponin I (TnI) was determined using nuclear magnetic resonance (NMR) spectroscopy. The solution structure determined by NMR is similar to the structure of the C-domain from intact TnC in complex with TnI(1)(-)(47) determined by X-ray crystallography [Vassylyev, D. G., Takeda, S., Wakatsuki, S., Maeda, K., and Maeda, Y. (1998) Proc. Natl. Acad. Sci. U.S.A. 95, 4847-4852]. Changes in the dynamic properties of CTnC.2Ca2+ induced by Rp40 binding were investigated using backbone amide (15)N NMR relaxation measurements. Analysis of NMR relaxation data allows for extraction of motional order parameters on a per residue basis, from which the contribution of changes in picosecond to nanosecond time scale motions to the conformational entropy associated with complex formation can be estimated. The results indicate that binding of Rp40 decreases backbone flexibility in CTnC, particularly at the end of the C-terminal helix. The backbone conformational entropy change (-TDeltaS) associated with binding of Rp40 to CTnC.2Ca2+ determined from (15)N relaxation data is 9.6 +/- 0.7 kcal mol(-1) at 30 degrees C. However, estimation of thermodynamic quantities using a structural approach [Lavigne, P., Bagu, J. R., Boyko, R., Willard, L., Holmes, C. F., and Sykes, B. D. (2000) Protein Sci. 9, 252-264] reveals that the change in solvation entropy upon complex formation is dominant and overcomes the thermodynamic "cost" associated with "stiffening" of the protein backbone upon Rp40 binding. Additionally, backbone amide (15)N relaxation data measured at different concentrations of CTnC.2Ca2+.Rp40 reveal that the complex dimerizes in solution. Fitting of the apparent global rotational correlation time as a function of concentration to a monomer-dimer equilibrium yields a dimerization constant of approximately 8.3 mM.

Literature references that cite this PDB file's key reference

  PubMed id Reference
  21465563 X.Xu, R.Ishima, and J.B.Ames (2011).
Conformational dynamics of recoverin's Ca(2+) -myristoyl switch probed by (15) N NMR relaxation dispersion and chemical shift analysis.
  Proteins, 79, 1910-1922.  
18942859 D.S.Pearson, D.R.Swartz, and M.A.Geeves (2008).
Fast pressure jumps can perturb calcium and magnesium binding to troponin C F29W.
  Biochemistry, 47, 12146-12158.  
17075134 O.K.Baryshnikova, and B.D.Sykes (2006).
Backbone dynamics of SDF-1alpha determined by NMR: interpretation in the presence of monomer-dimer equilibrium.
  Protein Sci, 15, 2568-2578.  
15930003 M.Ivancic, A.M.Spuches, E.C.Guth, M.A.Daugherty, D.E.Wilcox, and B.A.Lyons (2005).
Backbone nuclear relaxation characteristics and calorimetric investigation of the human Grb7-SH2/erbB2 peptide complex.
  Protein Sci, 14, 1556-1569.  
15826946 T.M.Blumenschein, D.B.Stone, R.J.Fletterick, R.A.Mendelson, and B.D.Sykes (2005).
Calcium-dependent changes in the flexibility of the regulatory domain of troponin C in the troponin complex.
  J Biol Chem, 280, 21924-21932.  
15711886 M.X.Li, X.Wang, and B.D.Sykes (2004).
Structural based insights into the role of troponin in cardiac muscle pathophysiology.
  J Muscle Res Cell Motil, 25, 559-579.  
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
12414713 P.Damberg, J.Jarvet, P.Allard, U.Mets, R.Rigler, and A.Gräslund (2002).
(13)C-(1)H NMR relaxation and fluorescence anisotropy decay study of tyrosine dynamics in motilin.
  Biophys J, 83, 2812-2825.  
11685229 M.Akke, and W.J.Chazin (2001).
An open and shut case.
  Nat Struct Biol, 8, 910-912.  
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.