Structural Effects of the GXXXG Motif on the Oligomer Formation of Transmembrane Domain of Syndecan-4

Bulletin of the Korean chemical society

Jooyoung Song¹  Ji-Sun Kim¹  Sung-Sub Choi¹  Yongae Kim¹ 

关键词: Syndecan-4;    Transmembrane;    GXXXG;    Oligomerization;    NMR spectroscopy;   

DOI  :  

学科分类：化学（综合）

来源: Korean Chemical Society

【 摘 要 】

Syndecan-4 (heparan sulfate proteoglycan), biologically important in cell-to-cell interactions and tumor suppression, was studied through mutation of the GXXXG motif of its transmembrane domain (Syd4-TM), a motif which governs dimerization. The expression and purification of the mutant (mSyd4-TM) were optimized here to assess the function of the GXXXG motif in the dimerization of Syd4-TM. mSyd4-TM was obtained in M9 minimal media and its oligomerization was identified by SDS PAGE, Circular Dichroism (CD) spectroscopy, mass spectrometry and NMR spectroscopy. The mutant, unlike Syd4-TM, did not form dimers and was observed as monomers. The GXXXG motif of Syd-4TM was shown to be an important structural determinant of its dimerization.

【 授权许可】

Unknown