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http://dx.doi.org/10.5012/bkcs.2008.29.5.1013

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)
Publication Information
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.
Keywords
Syndecan-3; Proteoglycan; NMR
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