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Solution structure of the cytoplasmic domain of syndecan-3 by two-dimensional NMR spectroscopy

Title
Solution structure of the cytoplasmic domain of syndecan-3 by two-dimensional NMR spectroscopy
Authors
Yeo, In YoungKoo, BonkyungOh, Eok-sooHan, Inn-OcLee, Weontae
Ewha Authors
오억수
SCOPUS Author ID
오억수scopus
Issue Date
2008
Journal Title
BULLETIN OF THE KOREAN CHEMICAL SOCIETY
ISSN
0253-2964JCR Link
Citation
vol. 29, no. 5, pp. 1013 - 1017
Keywords
syndecan-3proteoglycanNMR
Publisher
KOREAN CHEMICAL SOC
Indexed
SCI; SCIE; SCOPUS; KCI WOS scopus
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 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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자연과학대학 > 생명과학전공 > Journal papers
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