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| Type |
Poster Presentation |
| Area |
Life Chemistry |
| Room No. |
Exhibition Hall 2+3 |
| Time |
10월 19일 (목요일) 11:00~12:30 |
| Code |
BIO.P-275 |
| Subject |
NMR Structural analysis of syndecan-4 receptor |
| Authors |
Ji Sun Kim, YONGAE KIM*
Department of Chemistry, Hankuk University of Foreign Studies, Korea
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| Abstract |
Syndecan-4 is a widespread heparan sulfate proteoglycans also present in human mesenchymal cells, epithelia and endothelia, and is involved in focal adhesion assembly and cytoskeletal organization. In addition, the interaction of syndecan-4 with GFRs (growth factor receptors) is a very important factor in cancer progression and is particularly associated with resistance to treatment and therapy in breast cancer.
To get a better understanding of the mechanism and function of syndecan-4, it is crucial to investigate its three dimensional structure. Syndecan-4 comprises three major sections: extracellular (ecto-), transmembrane (TM) and cytoplasmic (Cyto-) domains. It also forms a dimer like the transmembrane domain of all syndecans forms homodimers by highly conserved GXXXG motifs. The cytoplasmic domain of syndecan-4 forms twisted dimers by the presence of PIP2 (phosphotidylinositol (4,5)-bisphosphate), which induces protein kinase Cα persistently binding and activation. Thus, the structural alteration of the transmembrane and cytoplasmic domains by binding with PKC-α and PIP2 regulates the function of the extracellular domain.
We obtained pure protein samples by expressing and purifying wild type Syd4-TM (wtSyd4), mutant Syd4-TM(mSyd4) and Syd4-eTC(ecto-, TM, Cyto-), respectively, for structural studies to understand the function of syndecan 4. And their structures were investigated by various spectroscopic methods as well as solution/solid-state NMR spectroscopy. |
| E-mail |
cucu860@daum.net |
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120th General Meeting of the KCS