Structure Determination of Syndecan-4 Transmembrane Domain using PISA Wheel Pattern and Molecular Dynamics simulation
0
조회
0
다운로드
1
인용
0
참고문헌
키워드
초록
Human transmembrane proteins (hTMPs) 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 hTMPs, 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 hTMPs. We tried to produce large amounts of Syndecan-4 transmembrane domain (Syd4-TM) that is related to the healing wounds and tumor for a long time. In this study, we performed the structure determination of Syd4-TM combining the Polarity Index at Slanted Angle (PISA) wheel pattern analysis based on 15N-1H 2D SAMPI-4 solid-state NMR of expressed Syd4-TM and Molecular Dynamics (MD) simulation using Discovery Studio 3.1.
Abstract
Human transmembrane proteins (hTMPs) 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 hTMPs, 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 hTMPs. We tried to produce large amounts of Syndecan-4 transmembrane domain (Syd4-TM) that is related to the healing wounds and tumor for a long time. In this study, we performed the structure determination of Syd4-TM combining the Polarity Index at Slanted Angle (PISA) wheel pattern analysis based on 15N-1H 2D SAMPI-4 solid-state NMR of expressed Syd4-TM and Molecular Dynamics (MD) simulation using Discovery Studio 3.1.
참고문헌 (11)
- S. E. Stringer, , Int. J. Biochem. Cell Biol, 29, pp.709~ (1997)
- G. David, , J. Cell. Biol, 118, pp.961~ (1992)
- K. Elenius, , J. Cell Sci, 107, pp.2975~ (1994)
- A. Horowitz, , J. Cell. Sci, 157, pp.715~ (2002)
- E. Okina, , Scand. J. Med. Sci. Sports, 19, pp.479~ (2009)
- M. Gulyás, , J. Pathol, 199, pp.479~ (2003)
- D. M. Beauvais, , Reprod. Biol. Endocrin, 2, pp.3~ (2004)
- Y. G. Park, , Reson.Soc, 16, pp.147~ (2012)
- A. A. Nevzorov, , J. Magn. Reson, 185, pp.59~ (2007)
- S. H. Park, , J. Mol. Biol, 333, pp.409~ (2003)
- E. L. Wu, , J. Comput. Chem, 35, pp.1997~ (2014)