By a News Reporter-Staff News Editor at Life Science Weekly -- Data detailed on Molecular Imaging have been presented. According to news reporting originating from Munster, Germany, by NewsRx correspondents, research stated, "The vertebrate sodium channel 3 subunit regulates channel behavior. The immunoglobulin domain of the human 3 subunit crystallizes as a trimer, and the full-length protein assembles as a trimer in vivo."
Our news editors obtained a quote from the research from the University of Munster, "Our results reveal an unexpected organization of the 3 subunit. A new structural insight into the sodium channel is presented. The vertebrate sodium (Na-v) channel is composed of an ion-conducting subunit and associated subunits. Here, we report the crystal structure of the human 3 subunit immunoglobulin (Ig) domain, a functionally important component of Na-v channels in neurons and cardiomyocytes. Surprisingly, we found that the 3 subunit Ig domain assembles as a trimer in the crystal asymmetric unit. Analytical ultracentrifugation confirmed the presence of Ig domain monomers, dimers, and trimers in free solution, and atomic force microscopy imaging also detected full-length 3 subunit monomers, dimers, and trimers. Mutation of a cysteine residue critical for maintaining the trimer interface destabilized both dimers and trimers. Using fluorescence photoactivated localization microscopy, we detected full-length 3 subunit trimers on the plasma membrane of transfected HEK293 cells. We further show that 3 subunits can bind to more than one site on the Na-v 1.5 subunit and induce the formation of subunit oligomers, including trimers."
According to the news editors, the research concluded: "Our results suggest a new and unexpected role for the 3 subunits in Na-v channel cross-linking and provide new structural insights into some pathological Na-v channel mutations."
For more information on this research see: Crystal Structure and Molecular Imaging of the Nav Channel beta 3 Subunit Indicates a Trimeric Assembly. Journal of Biological Chemistry, 2014;289(15):10797-10811. Journal of Biological Chemistry can be contacted at: Amer Soc Biochemistry Molecular Biology Inc, 9650 Rockville Pike, Bethesda, MD 20814-3996, USA. (American Society for Biochemistry and Molecular Biology - www.asbmb.org; Journal of Biological Chemistry - www.jbc.org/)
The news editors report that additional information may be obtained by contacting S. Namadurai, University of Munster, Inst Med Phys & Biophys, D-3148149 Munster, Germany. Additional authors for this research include D. Balasuriya, R. Rajappa, M. Wiemhofer, K. Stott, J. Klingauf, J.M. Edwardson, D.Y. Chirgadze and A.P. Jackson (see also Molecular Imaging).
Keywords for this news article include: Europe, Munster, Germany, Immunology, Immunoproteins, Nanotechnology, Immunoglobulins, Serum Globulins, Molecular Imaging, Emerging Technologies
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