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


Vol. 34,  No. 12, pp. 3577-3585, Dec.  2013
10.5012/bkcs.2013.34.12.3577


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  Abstract

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.

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  Cite this article

[IEEE Style]

J. Song, J. Kim, S. Choi, Y. Kim, "Structural Effects of the GXXXG Motif on the Oligomer Formation of Transmembrane Domain of Syndecan-4," Bulletin of the Korean Chemical Society, vol. 34, no. 12, pp. 3577-3585, 2013. DOI: 10.5012/bkcs.2013.34.12.3577.

[ACM Style]

Jooyoung Song, Ji-Sun Kim, Sung-Sub Choi, and Yongae Kim. 2013. Structural Effects of the GXXXG Motif on the Oligomer Formation of Transmembrane Domain of Syndecan-4. Bulletin of the Korean Chemical Society, 34, 12, (2013), 3577-3585. DOI: 10.5012/bkcs.2013.34.12.3577.

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ISSN(Print) 0253-2964
ISSN(Online) 1229-5949