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Science 22 February 1985:
Vol. 227. no. 4689, pp. 945 - 948
DOI: 10.1126/science.3969570
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Articles

Science, Vol 227, Issue 4689, 945-948
Copyright © 1985 by American Association for the Advancement of Science

articles

Molecular structure of troponin C from chicken skeletal muscle at 3-angstrom resolution

M Sundaralingam, R Bergstrom, G Strasburg, ST Rao, P Roychowdhury, M Greaser, and BC Wang

The x-ray structure of chicken skeletal muscle troponin C (TnC), the Ca2+-binding subunit of the troponin complex, shows that the protein is about 70 angstroms long with an unusual dumbbell shape. The carboxyl and amino domains are separated by a single long alpha helix of about nine turns. Only the two high-affinity Ca2+-Mg2+ sites of the COOH-domain are occupied by metal ions resulting in conformational differences between the COOH- and NH2-domains. These differences are probably important in the triggering of muscle contraction by TnC. Also the structure of TnC is relevant in understanding the function of other calcium-regulated proteins, in particular that of calmodulin because of its strong similarity in amino acid sequence.


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Blocking the Ca[IMAGE]-induced Conformational Transitions in Calmodulin with Disulfide Bonds.
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Kinetic Studies of Calcium Binding to the Regulatory Site of Troponin C from Cardiac Muscle.
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Ordered self-assembly of polypeptide fragments to form nativelike dimeric trp repressor.
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Crystallographic Structure of the Octamer Histone Core of the Nucleosome.
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Aromatic-aromatic interaction: a mechanism of protein structure stabilization.
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