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Science 20 July 1990:
Vol. 249. no. 4966, pp. 280 - 283
DOI: 10.1126/science.2374927
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Articles

Science, Vol 249, Issue 4966, 280-283
Copyright © 1990 by American Association for the Advancement of Science

articles

Calcium-induced peptide association to form an intact protein domain: 1H NMR structural evidence

GS Shaw, RS Hodges, and BD Sykes

Department of Biochemistry, University of Alberta, Edmonton, Canada.

The 70-residue carboxyl-terminal domain of the muscle contractile protein troponin-C contains two helix-loop-helix calcium (Ca)-binding sites that are related to each other by approximate twofold rotational symmetry. Hydrophobic residues from the helices and a short three residue beta sheet at the interface of the two sites act to stabilize the protein domain in the presence of Ca. A synthetic 34-residue peptide representing one of these sites (site III) has been synthesized and studied by H-1 nuclear magnetic resonance (NMR) spectroscopy. In solution this peptide undergoes a Ca-induced conformational change to form the helix-loop-helix Ca-binding motif. Two-dimensional nuclear Overhauser effect spectra have provided evidence for the formation of a beta sheet and interactions between several hydrophobic residues from opposing helices as found in troponin-C. It is proposed that a symmetric two-site dimer similar in tertiary structure to the carboxyl-terminal domain of troponin-C forms from the assembly of two site III peptides in the Ca-bound form.


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