The NMR angle on troponin C

1998 ◽  
Vol 76 (2-3) ◽  
pp. 302-312 ◽  
Author(s):  
Stéphane M Gagné ◽  
Monica X Li ◽  
Ryan T McKay ◽  
Brian D Sykes
Keyword(s):  
Calcium Binding ◽  
Structural Changes ◽  
Regulatory Protein ◽  
Protein Nmr ◽  
Troponin C ◽  
Structural Studies ◽  
Cardiac System ◽  
Helical Proteins ◽  
Central Paradigm ◽  
Concomitant Exposure

The calcium-induced structural changes in the skeletal muscle regulatory protein troponin C involve a transition from a closed to an open structure with the concomitant exposure of a large hydrophobic interaction site for target proteins. NMR solution structural studies have served to define this conformational change and elucidate the mechanism of the linkage between calcium binding and the induced structural changes. These structural movements are described in terms of interhelical angles in these largely helical proteins. Oddly, the most recent structure of the cardiac system challenges the central paradigm because the calcium-bound structures are not open. The kinetics, energetics, and dynamics of these proteins have also been investigated using NMR.Key words: troponin C, calcium binding protein, NMR, structure, energetics.

General discussion

1983 ◽  
Vol 302 (1108) ◽  
pp. 99-99
Keyword(s):  
Inorganic Chemistry ◽  
Calcium Binding ◽  
Troponin C ◽  
Chemistry Department ◽  
Helical Structures ◽  
Ef Hand ◽  
Helical Proteins ◽  
Information Energy ◽  
Positively Charged

R . J . P. Williams, F. R. S. (Inorganic Chemistry Department, Oxford, U. K. ) In the light of the frequent references at this meeting to the involvement of phosphorylation in modulating calcium triggering it is of interest to ask how this can come about when the sites of calcium binding and those of phosphorylation are far apart and often on different proteins. I shall attempt to answer this question on the basis of n.m.r. work by Dr B. A. Levine and myself. We know that calcium binding is to proteins of the EF-hand type, i.e. troponin-C and calmodulin. Calcium, as a positively charged ion, binds negatively charged loops of these helical proteins and subsequently the helical structures of the proteins are adjusted. We have shown that all the proteins behave in a very similar manner. The helix adjustments act as the transmission device for information (energy) from one end of a helix to another. These devices are well described by very detailed n.m.r. studies that we have summarized and will report in detail elsewhere.

scholarly journals Mutation of the high affinity calcium binding sites in cardiac troponin C.

1992 ◽  
Vol 267 (2) ◽  
pp. 825-831 ◽  
Author(s):  
J C Negele ◽  
D G Dotson ◽  
W Liu ◽  
H L Sweeney ◽  
J A Putkey
Keyword(s):  
Binding Sites ◽  
Calcium Binding ◽  
Cardiac Troponin ◽  
Troponin C ◽  
High Affinity ◽  
Cardiac Troponin C ◽  
Calcium Binding Sites

The amino acid sequence of porcine intestinal calcium-binding protein

1979 ◽  
Vol 57 (6) ◽  
pp. 737-748 ◽  
Author(s):  
Theo Hofmann ◽  
Michiko Kawakami ◽  
Anthony J. W. Hitchman ◽  
Joan E. Harrison ◽  
Keith J. Dorrington
Keyword(s):  
Mass Spectrometry ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Intestinal Mucosa ◽  
Calcium Binding ◽  
Binding Protein ◽  
Troponin C ◽  
Calcium Binding Protein ◽  
Mass Spectrometry Analysis ◽  
Spectrometry Analysis

The complete amino acid sequence of the calcium-binding protein (CaBP) from pig intestinal mucosa has been determined: Ac-Ser-Ala-Gln-Lys-Ser-Pro-Ala-Glu-Leu-Lys-Ser-Ile-Phe-Glu-Lys-Tyr-Ala-Ala-Lys-Glu-Gly-Asp-Pro-Asn-Gln-Leu-Ser-Lys-Glu-Glu-Leu-Lys-Gln-Leu-Ile-Gln-Ala-Glu-Phe-Pro-Ser-Leu-Leu-Lys-Gly-Pro-Arg-Thr-Leu-Asp-Asp-Leu-Phe-Gln-Glu-Leu-Asp-Lys-Asn-Gly-Asn-Gly-Glu-Val-Ser-Phe-Glu-Glu-Phe-Gln-Val-Leu-Val-Lys-Lys-Ile-Ser-Gln-OH. The N-terminal octapeptide sequence was determined by mass spectrometry analysis by Morris and Dell. The first 45 residues of bovine CaBP differ only in six positions from the corresponding sequence of the porcine protein, except that the sequence starts in position two of the porcine sequence. The mammalian intestinal CaBP's belong to the troponin-C superfamily on the basis of an analysis by Barker and Dayhoff.

Sign in / Sign up

Export Citation Format

Share Document