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PROTEIN STRUCTURE REPORT

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

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 calcium-binding. The backbone dynamics of the protein as measured by ¹⁵N relaxation rates and hetero-nuclear 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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