The x-ray structure of chicken skeletal muscle troponin C reveals a 70-angstrom dumbbell shape with a single long alpha helix separating the carboxyl and amino domains.
Molecular structure of troponin C
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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Sundaralingam et al. (Fri,) reported a other. The x-ray structure of chicken skeletal muscle troponin C reveals a 70-angstrom dumbbell shape with a single long alpha helix separating the carboxyl and amino domains.
synapsesocial.com/papers/6a21c83178057b574207bfbc — DOI: https://doi.org/10.1126/science.3969570
M. Sundaralingam
Scripps Research Institute
R. M. Bergström
University of Helsinki
Gale M. Strasburg
Michigan United
Science
University of Wisconsin–Madison
University of Pittsburgh Medical Center
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