1yx7
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(New page: 200px<br /><applet load="1yx7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1yx7" /> '''NMR structure of Calsensin, energy minimized...)
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Revision as of 04:59, 21 November 2007
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NMR structure of Calsensin, energy minimized average structure.
Overview
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.
About this Structure
1YX7 is a Single protein structure of sequence from Haemopis marmorata. Full crystallographic information is available from OCA.
Reference
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
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