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http://dx.doi.org/10.6564/JKMRS.2016.20.4.129

Structural Change in Transmembrane Region of Syndecan-4 by Mutation  

Choi, Sung-Sub (Department of Chemistry, Hankuk University of Foreign Studies)
Kim, Ji-Sun (Department of Chemistry, Hankuk University of Foreign Studies)
Jeong, Ji-Ho (Department of Chemistry, Hankuk University of Foreign Studies)
Kim, Yongae (Department of Chemistry, Hankuk University of Foreign Studies)
Publication Information
Journal of the Korean Magnetic Resonance Society / v.20, no.4, 2016 , pp. 129-137 More about this Journal
Abstract
Transmembrane(TM) proteins are closely related to transport, channel formation, signaling, cell to cell interaction, so they are the crucial target of modern medicinal drugs. In order to study the structure and function of these TM proteins, it is important to prepare reasonable amounts of proteins. However, their preparation is seriously difficult and time-consuming due to insufficient yields and low solubility of TM proteins. We tried to produce large amounts of Syndecan-4 containing TM domain(SDC4-TM) that is related to the wound healing and tumor. Also, mutated SDC4-TM was studied to investigate structural change by modification of dimerization motif. We performed the structure determination by the Polarity Index at Slanted Angle (PISA) wheel pattern analysis based on $^{15}N-^1H$ 2D SAMPI-4 solid-state NMR of SDC4-TM and computational modeling using Discovery Studio 2016.
Keywords
Solid-state NMR; Syndecan; Transmembrane; Membrane protein; Computational modeling;
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