Comparison of the crystal and solution structures of calmodulin and troponin C.

X-ray solution scattering data from skeletal muscle troponin C and from calmodulin have been measured. Modeling studies based on the crystal structure coordinates for these proteins show discrepancies between the solution data and the crystal structure that indicate that if the size and shape of the globular domains are the same in solution as in the crystal, the distances between them must be smaller by several angstroms. Bringing the globular domains closer together requires structural changes in the interconnecting helix that joins them.

[1]  M. Brillouin,et al.  La diffraction des rayons X aux très petits angles: application a l'étude de phénomènes ultramicroscopiques , 1939 .

[2]  Charles E. Bugg,et al.  Three-dimensional structure of calmodulin , 1985, Nature.

[3]  P. B. Moore,et al.  Small-angle scattering. Information content and error analysis , 1980 .

[4]  P. Charlier,et al.  Crystallization and structure at 3.2 Å resolution of a terbium parvalbumin , 1985 .

[5]  G. Balian,et al.  Collagen characterisation and cell transformation in human atherosclerosis , 1975, Nature.

[6]  F M Richards,et al.  Calcium-induced increase in the radius of gyration and maximum dimension of calmodulin measured by small-angle X-ray scattering. , 1985, Biochemistry.

[7]  T. Vanaman,et al.  The complete amino acid sequence of the Ca2+-dependent modulator protein (calmodulin) of bovine brain. , 1980, The Journal of biological chemistry.

[8]  K. Moffat,et al.  Structure of vitamin D-dependent calcium-binding protein from bovine intestine , 1981, Nature.

[9]  W. Y. Cheung,et al.  Calmodulin plays a pivotal role in cellular regulation. , 1980, Science.

[10]  M. Sundaralingam,et al.  Molecular structure of troponin C from chicken skeletal muscle at 3-angstrom resolution. , 1985, Science.

[11]  R. Kretsinger,et al.  Refinement of the structure of carp muscle calcium-binding parvalbumin by model building and difference Fourier analysis. , 1976, Journal of molecular biology.

[12]  M. Sundaralingam,et al.  Stabilization of the long central helix of troponin C by intrahelical salt bridges between charged amino acid side chains. , 1985, Proceedings of the National Academy of Sciences of the United States of America.

[13]  A. Means,et al.  Sequence homology of the Ca2+-dependent regulator of cyclic nucleotide phosphodiesterase from rat testis with other Ca2+-binding proteins. , 1978, The Journal of biological chemistry.

[14]  A. Means,et al.  Calmodulin—an intracellular calcium receptor , 1980, Nature.

[15]  J. Wilkinson.  The preparation and properties of the components of troponin B. , 1974, Biochimica et biophysica acta.

[16]  C. Kay,et al.  Comparative calcium binding and conformational studies of turkey and rabbit skeletal troponin C , 1986, FEBS Letters.

[17]  M. James,et al.  Structure of the calcium regulatory muscle protein troponin-C at 2.8 Å resolution , 1985, Nature.

[18]  G. Zaccaı̈,et al.  small angle neutron scattering , 2020, Catalysis from A to Z.