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Solution structure of the cytoplasmic domain of syndecan-3 by two-dimensional NMR spectroscopy
- Solution structure of the cytoplasmic domain of syndecan-3 by two-dimensional NMR spectroscopy
- Yeo, In Young; Koo, Bonkyung; Oh, Eok-soo; Han, Inn-Oc; Lee, Weontae
- Ewha Authors
- SCOPUS Author ID
- Issue Date
- Journal Title
- BULLETIN OF THE KOREAN CHEMICAL SOCIETY
- BULLETIN OF THE KOREAN CHEMICAL SOCIETY vol. 29, no. 5, pp. 1013 - 1017
- syndecan-3; proteoglycan; NMR
- KOREAN CHEMICAL SOC
- SCIE; SCOPUS; KCI
- Document Type
- 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 Cl 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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