Browse > Article

Detergent Screening for NMR-Based Structural Study of the Integral Membrane Protein, Emopamil Binding Protein (Human Sterol Δ8-Δ7 Isomerase)  

Won, Hyung-Sik (Department of Biotechnology, College of Biomedical and health Science, Konkuk University)
Publication Information
Journal of the Korean Magnetic Resonance Society / v.21, no.1, 2017 , pp. 13-19 More about this Journal
Human sterol ${\Delta}8-{\Delta}7$ isomerase, commonly known as emopamil binding protein (EBP), is an essential protein in the cholesterol-synthetic pathway, and mutations of this protein are critically associated with human diseases such as Conradi-Hunermann-Happle or male EBP disorder with neurological defects syndrome. Due to such a clinical importance, EBP has been intensively investigated and some important features have been reported. EBP is a tetra-spanning membrane protein, of which $2^{nd}$, $3^{rd}$, and $4^{th}$ membrane-spanning ${\alpha}$ helices play an important role in its enzymatic function. However, detailed structural feature at atomic resolution has not yet been elucidated, due to characteristic difficulties in dealing with membrane protein. Here, we over-expressed EBP using Escherichia coli and performed detergent screening to find suitable membrane mimetics for structural studies of the protein by NMR. As results, DPC and LMPG could be evaluated as the most favorable detergents to acquire promising NMR spectra for structural study of EBP.
emopamil binding protein; cholesterol; sterol ${\Delta}8-{\Delta}7$ isomerase; detergent screening; NMR;
Citations & Related Records
Times Cited By KSCI : 2  (Citation Analysis)
연도 인용수 순위
1 L. X. Finegold, Cholesterol in membrane models, CRC Press (1992)
2 P. L. Yeagle, Biochimie 73, 1303 (1991)   DOI
3 P. L. Yeagle, Biochim. Biophys. Acta 822, 267 (1985)   DOI
4 L. J. Sharpe, and A. J. Brown, J. Biol. Chem. 288, 18707 (2013)   DOI
5 A. A. Kandutsch, and A. E. Russell, J. Biol. Chem. 235, 2256 (1960)
6 K. Bloch, Steroids 57, 378 (1992)   DOI
7 L. V. Furtado, P. Bayrak-Toydemir, B. Hulinsky, K. Damjanovich, J. C. Carey, and A. F. Rope, Am. J. Med. Genet. 152A, 2838 (2010)   DOI
8 A. Kolb-Maurer, K. H. Grzeschik, D. Haas, E. B. Brocker, and H. Hamm, Acta Derm-Venereol. 88, 47 (2008)   DOI
9 B. U. Fitzky, M. Witsch-Baumgartner, M. Erdel, J. N. Lee, Y. K. Paik, H. Glossmann, G. Utermann, and F. F. Moebius, Proc. Natl. Acad. Sci. U.S.A. 95, 8181 (1998)   DOI
10 F. F. Moebius, G. G. Burrows, J. Striessnig, and H. Glossmann, Mol. Pharmacol. 43, 139 (1993)
11 F. F. Moebius, M. Hanner, H. G. Knaus, F. Weber, J. Striessnig, and H. Glossmann, J. Biol. Chem. 269, 29314 (1994)
12 M. Hanner, F. F. Moebius, F. Weber, M. Grabner, J. Striessnig, and H. Glossmann, J. Biol. Chem. 270, 7551 (1995)   DOI
13 F. F. Moebius, R. J. Reiter, K. Bermoser, H. Glossmann, S. Y. Cho, and Y. K. Paik, Mol. Pharmacol. 54, 591 (1998)   DOI
14 S. Silve, P. H. Dupuy, C. Labit-Lebouteiller, M. Kaghad, P. Chalon, A. Rahier, M. Taton, J. Lupker, D. Shire, and G. Loison, J. Biol. Chem. 271, 22434 (1996)   DOI
15 S. Silve, P. Leplatois, A. Josse, P. H. Dupuy, C. Lanau, M. Kaghad, C. Dhers, C. Picard, A. Rahier, M. Taton, G. Le Fur, D. Caput, P. Ferrara, and G. Loison, Mol. Cell. Biol. 16, 2719 (1996)   DOI
16 F. F. Moebius, K. E. Soellner, B. Fiechtner, C. W. Huck, G. Bonn, and H. Glossmann, Biochemistry 38, 1119 (1999)   DOI
17 A. Rahier, S. Pierre, G. Riveill, and F. Karst, Biochem. J. 414, 247 (2008)   DOI
18 A. Korepanova, F. P. Gao, Y. Hua, H. Qin, R. K. Nakamoto, and T. A. Cross, Protein Sci. 14, 148 (2005)
19 M. Renault, O. Saurel, P. Demange, V. Reat, and A. Milon, Methods Mol. Biol. 654, 321 (2010)
20 B. Liang, and L. K. Tamm, Proc. Natl. Acad. Sci. U.S.A. 104, 16140 (2007)   DOI
21 R. C. Page, J. D. Moore, H. B. Nguyen, M. Sharma, R. Chase, F. P. Gao, C. K. Mobley, C. R. Sanders, L. Ma, F. D. Sonnichsen, S. Lee, S. C. Howell, S. J. Opella, and T. A. Cross, J. Struct. Funct. Genomics 7, 51 (2006)   DOI
22 Y.-S. Lee, D.-W. Sim, M.-D. Seo, H-S. Won, and J.-H. Kim, J. Kor. Magn. Reson. Soc. 19, 137 (2015)   DOI
23 S. Bak, S.-J. Kang, T. Suzuki, M. Yoshida, T. Fujiwara, and H. Akutsu, J. Kor. Magn. Reson. Soc. 17, 67 (2013)   DOI
24 L. Columbus, J. Lipfert, K. Jambunathan, D. A. Fox, A. Y. Sim, S. Doniach, and S. A. Lesley, J. Am. Chem. Soc. 131, 7320 (2009)   DOI
25 D. Nietlispach, J. Biomol. NMR 31, 161 (2005)   DOI
26 F. Delaglio, S. Grzesiek, G. W. Vuister, G. Zhu, J. Pfeifer, and A. Bax, J. Biomol. NMR 6, 277 (1995)
27 T. Goddard and D. Kneller, SPARKY 3, University of California, San Francisco (2008)