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Published online before print June 3, 2005, 10.1110/ps.051412605
Protein Science (2005), 14:1894-1901. Published by Cold Spring Harbor Laboratory Press. Copyright © 2005 The Protein Society
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PROTEIN STRUCTURE REPORT

Solution structure and backbone dynamics of Calsensin, an invertebrate neuronal calcium-binding protein

Deepa V. Venkitaramani, D. Bruce Fulton, Amy H. Andreotti, Kristen M. Johansen and Jørgen Johansen

Department of Biochemistry, Biophysics, and Molecular Biology, Iowa State University, Ames, Iowa 50011, USA

(RECEIVED February 15, 2005; FINAL REVISION April 10, 2005; ACCEPTED April 11, 2005)

Calsensin is an EF-hand calcium-binding protein expressed by a subset of peripheral sensory neurons that fasciculate into a single tract in the leech central nervous system. Calsensin is a 9-kD protein with two EF-hand calcium-binding motifs. Using multidimensional NMR spectroscopy we have determined the solution structure and backbone dynamics of calcium-bound Calsensin. Calsensin consists of four helices forming a unicornate-type four-helix bundle. The residues in the third helix undergo slow conformational exchange indicating that the motion of this helix is associated with calciumbinding. The backbone dynamics of the protein as measured by 15N relaxation rates and heteronuclear NOEs correlate well with the three-dimensional structure. Furthermore, comparison of the structure of Calsensin with other members of the EF-hand calcium-binding protein family provides insight into plausible mechanisms of calcium and target protein binding.

Keywords: Calsensin; calcium-binding proteins; EF-hand; NMR structure; dynamics; helix–loop–helix; nervous system

Article published online ahead of print. Article and publication date are at http://www.proteinscience.org/cgi/doi/10.1110/ps.051412605.

Reprint requests to: Jørgen Johansen, Department of Biochemistry, Biophysics, and Molecular Biology, 3156 Molecular Biology Building, Iowa State University, Ames, IA 50011, USA; e-mail: jorgen{at}iastate.edu; fax: (515) 294-4858.


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