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Solution structure and main chain dynamics of the regulatory domain (Residues 1-91) of human cardiac troponin C

Pääkkönen, Kimmo; Annila, Arto; Sorsa, Tia; Pollesello, Piero; Tilgmann, Carola LU ; Kilpeläinen, Ilkka; Karisola, Piia; Ulmanen, Ismo and Drakenberg, Torbjörn LU (1998) In Journal of Biological Chemistry 273(25). p.15633-15638
Abstract

Thee three-dimensional structure of calcium-loaded regulatory, i.e. N- terminal, domain (1-91) of human cardiac troponin C (cNTnC) was determined by NMR in water/trifluoroethanol (91:9 v/v) solution. The single-calcium-loaded cardiac regulatory domain is in a 'closed' conformation with comparatively little exposed hydrophobic surface. Difference distance matrices computed from the families of Ca2+-cNTnC, the apo and two-calcium forms of the skeletal TnC (sNTnC) structures reveal similar relative orientations for the N, A, and D helices. The B and C helices are closer to the NAD framework in Ca2+-cNTnC and in apo-sNTnC than in 2-Ca2+sNTnC. However, there is an indication of a conformational exchange based... (More)

Thee three-dimensional structure of calcium-loaded regulatory, i.e. N- terminal, domain (1-91) of human cardiac troponin C (cNTnC) was determined by NMR in water/trifluoroethanol (91:9 v/v) solution. The single-calcium-loaded cardiac regulatory domain is in a 'closed' conformation with comparatively little exposed hydrophobic surface. Difference distance matrices computed from the families of Ca2+-cNTnC, the apo and two-calcium forms of the skeletal TnC (sNTnC) structures reveal similar relative orientations for the N, A, and D helices. The B and C helices are closer to the NAD framework in Ca2+-cNTnC and in apo-sNTnC than in 2-Ca2+sNTnC. However, there is an indication of a conformational exchange based on bread 15N resonances for several amino acids measured at several temperatures. A majority of the Amides in the α-helices and in the calcium binding loop exhibit very fast motions with comparatively small amplitudes according to the LipariSzabo model. A few residues at the N and C termini are flexible. Data were recorded from nonlabeled and 15N-labeled samples, and backbone dynamics was investigated by 15N T1, T2, and heteronuclear nuclear Overhauser effect as well as by relaxation interference measurements.

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author
publishing date
type
Contribution to journal
publication status
published
in
Journal of Biological Chemistry
volume
273
issue
25
pages
6 pages
publisher
American Society for Biochemistry and Molecular Biology
external identifiers
  • Scopus:0032546788
ISSN
0021-9258
DOI
10.1074/jbc.273.25.15633
language
English
LU publication?
no
id
f7f4ca3f-8e18-410f-8844-fad03d3670cc
date added to LUP
2016-04-11 13:16:57
date last changed
2016-10-13 05:05:47
@misc{f7f4ca3f-8e18-410f-8844-fad03d3670cc,
  abstract     = {<p>Thee three-dimensional structure of calcium-loaded regulatory, i.e. N- terminal, domain (1-91) of human cardiac troponin C (cNTnC) was determined by NMR in water/trifluoroethanol (91:9 v/v) solution. The single-calcium-loaded cardiac regulatory domain is in a 'closed' conformation with comparatively little exposed hydrophobic surface. Difference distance matrices computed from the families of Ca<sup>2+</sup>-cNTnC, the apo and two-calcium forms of the skeletal TnC (sNTnC) structures reveal similar relative orientations for the N, A, and D helices. The B and C helices are closer to the NAD framework in Ca<sup>2+</sup>-cNTnC and in apo-sNTnC than in 2-Ca<sup>2+</sup>sNTnC. However, there is an indication of a conformational exchange based on bread <sup>15</sup>N resonances for several amino acids measured at several temperatures. A majority of the Amides in the α-helices and in the calcium binding loop exhibit very fast motions with comparatively small amplitudes according to the LipariSzabo model. A few residues at the N and C termini are flexible. Data were recorded from nonlabeled and <sup>15</sup>N-labeled samples, and backbone dynamics was investigated by <sup>15</sup>N T<sub>1</sub>, T<sub>2</sub>, and heteronuclear nuclear Overhauser effect as well as by relaxation interference measurements.</p>},
  author       = {Pääkkönen, Kimmo and Annila, Arto and Sorsa, Tia and Pollesello, Piero and Tilgmann, Carola and Kilpeläinen, Ilkka and Karisola, Piia and Ulmanen, Ismo and Drakenberg, Torbjörn},
  issn         = {0021-9258},
  language     = {eng},
  month        = {06},
  number       = {25},
  pages        = {15633--15638},
  publisher    = {ARRAY(0xb32f9f0)},
  series       = {Journal of Biological Chemistry},
  title        = {Solution structure and main chain dynamics of the regulatory domain (Residues 1-91) of human cardiac troponin C},
  url          = {http://dx.doi.org/10.1074/jbc.273.25.15633},
  volume       = {273},
  year         = {1998},
}