Structural highlights
Function
CLSS_HAEMA May function as a trigger protein which interacts with a larger protein. May mediate calcium-dependent signal transduction events in the growth cones and axons of a small group of sensory neurons which fasciculate in a single axon tract.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
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 (15)N 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.
Solution structure and backbone dynamics of Calsensin, an invertebrate neuronal calcium-binding protein.,Venkitaramani DV, Fulton DB, Andreotti AH, Johansen KM, Johansen J Protein Sci. 2005 Jul;14(7):1894-901. Epub 2005 Jun 3. PMID:15937283[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Venkitaramani DV, Fulton DB, Andreotti AH, Johansen KM, Johansen J. Solution structure and backbone dynamics of Calsensin, an invertebrate neuronal calcium-binding protein. Protein Sci. 2005 Jul;14(7):1894-901. Epub 2005 Jun 3. PMID:15937283 doi:10.1110/ps.051412605
