Bulletin of the Korean Chemical Society

Korean Chemical Society (대한화학회)
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Solution Structure of the Cytoplasmic Domain of Syndecan-3 by Two-dimensional NMR Spectroscopy

  • Yeo, In-Young (Department of Biochemistry and Protein Network Research Center, Yonsei University) ;
  • Koo, Bon-Kyung (Department of Biochemistry and Protein Network Research Center, Yonsei University) ;
  • Oh, Eok-Soo (Department of Life Sciences, Division of Life and Pharmaceutical Sciences and the Center for Cell Signaling & Drug Discovery Research, Ewha Womans University) ;
  • Han, Inn-Oc (Department of Physiology and Biophysics, Inha University) ;
  • Lee, Weon-Tae (Department of Biochemistry and Protein Network Research Center, Yonsei University)
  • Published : 2008.05.20
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Abstract

Syndecan-3 is a cell-surface heparan sulfate proteoglycan, which performs a variety of functions during cell adhension process. It is also a coreceptor for growth factor, mediating cell-cell and cell-matrix interaction. Syndecan-3 contains a cytoplasmic domain potentially associated with the cytoskeleton. Syndecan-3 is specifically expressed in neuron cell and has related to neuron cell differentiation and development of actin filament in cell migration. Syndecans each have a unique, central, and variable (V) region in their cytoplasmic domains. And that region of syndecan-3 may modulate the interactions of the conserved C1 regions of the cytoplasmic domains by tyrosine phosphorylation. Cytoplasmic domain of syndecan-3 has been synthesized for NMR structural studies. The solution structure of syndecan-3 cytoplasmic domain has been determined by two-dimensional NMR spectroscopy and simulated-annealing calculation. The cytoplasmic domain of the syndecan proteins has a tendency to form a dimmer conformation with a central cavity, however, that of syndecan-3 demonstrated a monomer conformation with a flexible region near C-terminus. The structural information might add knowledge about the structure-function relationships among syndecan proteins.

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