Quantification of the calcium‐induced secondary structural changes in the regulatory domain of troponin‐C

Gagné, Stéphane M.; Tsuda, Sakae; Li, Monica X.; Chandra, Murali; Smillie, Lawrence B.; Sykes, Brian D.

doi:10.1002/pro.5560031108

Cited by 181 publications

(200 citation statements)

References 64 publications

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“…4); and (2) a N ( i , i ) / a N (i -1, i ) ratios that are significantly greater than 1 for residues in the a helix, and less than 1 for residues in &sheet regions. This is significant because this ratio tends to approach unity as the amount of spin diffusion increases (Gagne et al, 1994).…”

Section: Secondary Structure Determinationmentioning

confidence: 99%

“…In these experiments, statistically, only NOEs between "N-attached protons within asinglesubunif are observed. These NOE data, summarized in Figure 5 , are categorized as strong, medium, or weak after normalization of the cross peak heights with respect to those of the corresponding NH diagonal resonance to correct for NH peak height differences (Gagne et al, 1994). Evidence against significant spin-diffusion effects in the 50-ms NOESY spectra includes: (1) the absence of NN (i, i + 3) correlations in the a-helical region (Fig.…”

Section: Secondary Structure Determinationmentioning

confidence: 99%

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4‐Oxalocrotonate tautomerase, a 41‐kDa homohexamer: Backbone and side‐chain resonance assignments, solution secondary structure, and location of active site residues by heteronuclear NMR spectroscopy

Stivers¹,

Abeygunawardana²,

Whitman³

et al. 1996

Protein Science

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Abstract4-Oxalocrotonate tautomerase (4-OT), a homohexamer consisting of 62 residues per subunit, catalyzes the isomerization of unsaturated a-keto acids using Pro-1 as a general base (Stivers et al., 1996a(Stivers et al., , 1996b. We report the backbone and side-chain 'H, "N, and I3C NMR assignments and the solution secondary structure for 4-OT using 2D and 3D homonuclear and heteronuclear NMR methods. The subunit secondary structure consists of an a-helix (residues 13-30), two 0-strands (PI, residues 2-8; &, residues 39-45), a @-hairpin (residues 50-57), two loops (I, residues 9-12; 11, 34-38), and two turns (I, residues 30-33; II,47-50). The remaining residues form coils. The PI strand is parallel to the pz strand of the same subunit on the basis of cross strand NHi-NHj NOEs in a 2D "N-edited 'H-NOESY spectrum of hexameric 4-OT containing two I5N-labeled subunits/hexamer. The 0' strand is also antiparallel to another PI strand from an adjacent subunit forming a subunit interface. Because only three such pairwise interactions are possible, the hexamer is a trimer of dimers. The diffusion constant, determined by dynamic light scattering, and the rotational correlation time (14.5 ns) estimated from I5N T l / T , measurements, are consistent with the hexameric molecular weight of 41 kDa. Residue Phe-50 is in the active site on the basis of transferred NOEs to the bound partial substrate 2-0~0-1,6-hexanedioate. Modification of the general base, Pro-1, with the active site-directed irreversible inhibitor, 3-bromopyruvate, significantly alters the amide I5N and NH chemical shifts of residues in the 0-hairpin and in loop 11, providing evidence that these regions change conformation when the active site is occupied.

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Section: Secondary Structure Determinationmentioning

confidence: 99%

Section: Secondary Structure Determinationmentioning

confidence: 99%

4‐Oxalocrotonate tautomerase, a 41‐kDa homohexamer: Backbone and side‐chain resonance assignments, solution secondary structure, and location of active site residues by heteronuclear NMR spectroscopy

Stivers¹,

Abeygunawardana²,

Whitman³

et al. 1996

Protein Science

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“…The N-terminal Ser2ϪSer5 had coupling constants of 8.0 Hz or more, which was also indicated by high [47]. Grey bars indicate local secondary structure based on a ratio of NOE intensities [44]. Positive and negative bars denote β-conformation and helix, respectively.…”

Section: Resultsmentioning

confidence: 98%

“…These restraints were derived from the ratio of the d AN (i,iϩ1) and d NA (iϩ1,iϩ1) NOE volumes [44]. Ratios could be calculated for 20 residues, but were only used if (a) the volumes were not suspected to be unequally affected by solvent signal suppression, (b) the NOEs showed no overlap and (c) the corresponding distance ratio differed from 1 by more than 2.5 %, which resulted in 16 dihedral ψ-angle intervals.…”

Section: Methodsmentioning

confidence: 99%

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The solution structure of human endothelin‐2 a ¹H‐NMR and CD study

Arvidsson¹,

Nemoto²,

Mitsui³

et al. 1998

European Journal of Biochemistry

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The solution structure of the vasoactive endogenous 21-amino-acid human endothelin-2 has been determined by NMR and CD techniques, in a mixed solvent of 100 mM aqueous acetic acid and 25% (by vol.) 1,1,1,3,3,3-hexafluoro-2-propanol. From NMR-derived restraints on upper limit distances and dihedral angles, distance geometry structures were calculated using the program DADAS90, and refined by simulated annealing in X-PLOR. The structure of endothelin-2 consists of an A-helix of residues 9 to 17, orientated anti-parallel to a short β-strand of residues 1 to 3, linked together by a possible β-turn type I of residues 5Ϫ8. These secondary structural elements are stabilised and positioned by two disulphide bonds between residues 1 and 15, and 3 and 11, respectively. The average root mean square deviation over residues 1Ϫ17 of 15 accepted low-energy conformers chosen to reflect the solution structure of endothelin-2, was 0.73 Å for the backbone and 1.41 Å for all heavy atoms. The data on endothelin-2 will be discussed and compared with what has been published on other endothelin/sarafotoxin peptides.Keywords : endothelin-2; NMR; circular dichroism ; solution structure ; helix.Endothelin-1 was first isolated from porcine aortic endothelial cells [1]. The human genes encoding this peptide and two isoforms, endothelin-2 and endothelin-3, have been encountered and cloned [2]. From analysis of a mouse genome another peptide called vasoactive intestinal contractor (VIC) was identified [3]. These four mammalian peptides are strongly homologous ( Fig. 1). Moreover, they have pronounced sequence similarities with the snake venom sarafotoxins [4] and Bibrotoxin [5]. For this reason they have been suggested to form an endothelin/sarafotoxin peptide family. These peptides have 21 residues and two disulphide bonds connecting residues 1 and 15, and 3 and 11, respectively. They are also noted for evoking similar biological actions [6].The endothelin peptides were first characterised as being the most potent constrictors of smooth muscle. They are now known to produce a variety of pharmacological effects in various vascular and non-vascular tissues and to show numerous activities in the central and peripheral nervous systems. They have been linked to regulation of blood flow and to a number of diseases such as vasospasm, hypertension, myocardial infarction, arteriosclerosis and renal failure [7]. The role as a vasoconstrictor has however been questioned after a finding that blood pressure of transgenic 'knock-out' mice with only one copy of the gene, is somewhat raised, rather than lowered as was expected [8]. Disruption of both copies of the gene results in an embryonic lethal phenotype with malformed craniofacial organs [8].Two G-protein-coupled endothelin receptors have been characterised and cloned in mammalian species, ET A and ETB [9,Correspondence to H. Nakanishi, Biomolecular Chemistry Laboratory, Department of Biomolecules, National Institute of Bioscience and Human-Technology (NIBH), 1-1 Higashi, Tsukuba, Ibaraki, Japan 305-8...

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TroponinC

Gagn��

2004

Handbook of Metalloproteins

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Regulation of contraction in skeletal and cardiac muscle occurs through calcium binding to the protein troponin C (TnC). The N‐terminal domain of TnC (NTnC) carries out the regulatory role through the binding of calcium ions – two calcium ions in skeletal muscle and one in cardiac muscle. Thirty‐nine sequences of TnC have been sequenced so far. Of the 39 sequences of TnC, 5 have had their three‐dimensional structures determined in various forms by NMR and X‐ray. Available structures include 26 uncomplexed structures in various calcium states, and 13 structures in which cardiac and skeletal TnC is complexed with fragments of troponin I and/or troponin T.

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Quantification of the calcium‐induced secondary structural changes in the regulatory domain of troponin‐C

Cited by 181 publications

References 64 publications

4‐Oxalocrotonate tautomerase, a 41‐kDa homohexamer: Backbone and side‐chain resonance assignments, solution secondary structure, and location of active site residues by heteronuclear NMR spectroscopy

4‐Oxalocrotonate tautomerase, a 41‐kDa homohexamer: Backbone and side‐chain resonance assignments, solution secondary structure, and location of active site residues by heteronuclear NMR spectroscopy

The solution structure of human endothelin‐2 a ¹H‐NMR and CD study

TroponinC

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Quantification of the calcium‐induced secondary structural changes in the regulatory domain of troponin‐C

Cited by 181 publications

References 64 publications

4‐Oxalocrotonate tautomerase, a 41‐kDa homohexamer: Backbone and side‐chain resonance assignments, solution secondary structure, and location of active site residues by heteronuclear NMR spectroscopy

4‐Oxalocrotonate tautomerase, a 41‐kDa homohexamer: Backbone and side‐chain resonance assignments, solution secondary structure, and location of active site residues by heteronuclear NMR spectroscopy

The solution structure of human endothelin‐2 a 1H‐NMR and CD study

TroponinC

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The solution structure of human endothelin‐2 a ¹H‐NMR and CD study