Acta NaturaeActa NaturaeActa Naturae2075-8251Acta Naturae Ltd1068110.32607/20758251-2011-3-2-90-98ArticlesСтатьиResearch ArticleDimeric Structure of the Transmembrane Domain of Glycophorin A in Lipidic and Detergent EnvironmentsDimeric Structure of the Transmembrane Domain of Glycophorin A in Lipidic and Detergent EnvironmentsMineevK SBocharovE Vbon@nmr.ruVolynskyP EGoncharukM VTkachE NErmolyukYa SSchulgaA AChupinV VMaslennikovI VEfremovR GArsenievA SShemyakin and Ovchinnikov Institute of Bioorganic Chemistry, Russian Academy of Sciences1506201132VOL 3, NO2 (2011)ТОМ 3, №2 (2011)909817012020Copyright ©; 2011, Mineev K.S., Bocharov E.V., Volynsky P.E., Goncharuk M.V., Tkach E.N., Ermolyuk Y.S., Schulga A.A., Chupin V.V., Maslennikov I.V., Efremov R.G., Arseniev A.S.Copyright ©; 2011, Mineev K.S., Bocharov E.V., Volynsky P.E., Goncharuk M.V., Tkach E.N., Ermolyuk Y.S., Schulga A.A., Chupin V.V., Maslennikov I.V., Efremov R.G., Arseniev A.S.2011Mineev K.S., Bocharov E.V., Volynsky P.E., Goncharuk M.V., Tkach E.N., Ermolyuk Y.S., Schulga A.A., Chupin V.V., Maslennikov I.V., Efremov R.G., Arseniev A.S.Mineev K.S., Bocharov E.V., Volynsky P.E., Goncharuk M.V., Tkach E.N., Ermolyuk Y.S., Schulga A.A., Chupin V.V., Maslennikov I.V., Efremov R.G., Arseniev A.S.https://creativecommons.org/licenses/by/4.0https://actanaturae.ru/2075-8251/article/view/10681

Specific interactions between transmembrane α-helices, to a large extent, determine the biological function of integral membrane proteins upon normal development and in pathological states of an organism. Various membrane-like media, partially those mimicking the conditions of multicomponent biological membranes, are used to study the structural and thermodynamic features that define the character of oligomerization of transmembrane helical segments. The choice of the composition of the membrane-mimicking medium is conducted in an effort to obtain a biologically relevant conformation of the protein complex and a sample that would be stable enough to allow to perform a series of long-term experiments with its use. In the present work, heteronuclear NMR spectroscopy and molecular dynamics simulations were used to demonstrate that the two most widely used media (detergent DPC micelles and lipid DMPC/DHPC bicelles) enable to perform structural studies of the specific interactions between transmembrane a-helices by the example of dimerizing the transmembrane domain of the bitopic protein glycophorin A. However, a number of peculiarities place lipid bicelles closer to natural lipid bilayers in terms of their physical properties.

bitopic membrane proteinstransmembrane domaindimerizationspatial structuremolecular dynamicsNMRFrishman D., Mewes H.-W. // Prog. Biophys. Mol. Biol. 1999. V. 72. P. 1-17.Li E., Hristova K. // Biochemistry. 2006. V. 45. P. 6241-6251.Zviling M., Kochva U., Arkin I.T. // Biochim. Biophys. Acta. 2007. V. 1768. P. 387-392.Bocharov E.V., Volynsky P.E., Pavlov K.V., Efremov R.G., Arseniev A.S. // Cell Adh. Migr. 2010. V. 4. P. 284-298.Kim H.J., Howell S.C., van Horn W.D., Jeon Y.H., Sanders C.R. // Prog. Nucl. Magn. Reson. Spectrosc. 2009. V. 55. P. 335-360.MacKenzie K.R., Prestegard J.H., Engelman D.M. // Science. 1997. V. 276. P. 131-133.Smith S.O., Song D., Shekar S., Groesbeek M., Ziliox M., Aimoto S. // Biochemistry. 2001. V. 40. P. 6553-6558.Smith S.O., Eilers M., Song D., crocker E., Ying W., Groesbeek M., Metz G., Ziliox M., Aimoto S. // Biophys. J. 2002. V. 82. P. 2476-2486.Goncharuk M.V., Schulga A.A., Ermolyuk Ya.S., Tkach E.N., Goncharuk S.A., Pustovalova Yu.E., Mineev K.S., Bocharov E.V., Maslennikov I.V., Arseniev A.S., Kirpichnikov M.P. // Mol. Biol. (Mosk). 2011. V. 45. N 4. in press.Kirpichnikov M.P., Goncharuk M.V., Ermolyuk Ya.S., Goncharuk S.A., Schulga A.A. Maslennikov I.V., Arseniev A.S. // Technol. Live Syst. 2005. V. 2. P. 20-27.chakrabarti P., Khorana G. // Biochemistry. 1975. V. 14. P. 5021-5033.Sreerama N., Woody R.W. // Anal. Biochem. 2000. V. 287. P. 252-260.Keller R.L.J. The computer aided resonance assignment tutorial. Goldau, Switzerland: cANTINA Verlag, 2004. 81 p.cavanagh J., Fairbrother W. J., Palmer A.G., Skelton N.J. Protein NMR spectroscopy: principles and practice. 2nd ed. San Diego, cA, USA: Acad. Press, 2007. 886 p.Zwahlen C., Legault P., Vincent S.J.F., Greenblatt J., Konrat R., Kay L.E. // Am. chem. Soc. 1997. V. 119. P. 6711-6721.Bocharov E.V., Korzhnev D.M., Blommers M.J., Arvinte T., Orekhov V.Y., Billeter M., Arseniev A.S. // J. Biol. chem. 2002. V. 277. P. 46273-46279.Guntert P. // Prog. Nucl. Magn. Reson. Spectrosc. 2003. V. 43. P. 105-125.cornilescu G., Delaglio F., Bax A. // J. Biomol. NMR. 1999. V. 13. P. 289-302.Baker E.N., Hubbard R.E. // Prog. Biophys. Mol. Biol. 1984. V. 44. P. 97-179.Lindahl E., Hess B., van der Spoel D. // J. Mol. Mod. 2001. V. 7. P. 306-317.Bocharov E.V., Mayzel M.L., Volynsky P.E., Mineev K.S., Tkach E.N., Ermolyuk Ya.S., Schulga A.A., Efremov R.G., Arseniev A.S. // Biophys. J. 2010. V. 98. P. 881-889.Koradi R., Billeter M., Wuthrich K.J. // Mol. Graphics. 1996. V. 14. P. 51-55.DeLano W.L. The PyMOL Molecular Graphics System, Palo Alto, CA, USA: DeLano Scientific, 2002.Efremov R.G., Gulyaev D.I., Vergoten G., Modyanov N.N. // J. Prot. chem. 1992. V. 11. P. 665-675.Kabsch W., Sander C. // Biopolymers. 1983. V. 22. P. 2577-2637.Daragan V.A., Mayo K.H. // Prog. Nucl. Magn. Reson. Spectrosc. 1997. V. 31. P. 63-105.Bordag N., Keller S. // chem. Phys. Lipids. 2010. V. 163. P. 1-26.Lind J., Nordin J., Maler L. // Biochim. Biophys. Acta. 2008. V. 1778. P. 2526-2534.Nyholm T.K., Ozdirekcan S., Killian J.A. // Biochemistry. 2007. V. 46. P. 1457-1465.Sparr E., Ash W.L., Nazarov P.V., Rijkers D.T., Hemminga M.A., Tieleman D.P., Killian J.A. // J. Biol. chem. 2005. V. 280. P. 39324-39331.Mackenzie K.R. // Chem. Rev. 2006. V. 106. P. 1931-1977.Kim S., Jeon T.-J., Oberai A., Yang D., Schmidt J. J., Bowie J.U. // Proc. Natl. Acad. Sci. USA. 2005. V. 102. P. 14279-14283.Efremov R.G., Vereshaga Y.A., Volynsky P.E., Nolde D.E., Arseniev A.S. // J. Comput. Aided. Mol. Des. 2006. V. 20. P. 27-45.Senes A., Ubarretxena-Belandia I., Engelman D.M. // Proc. Natl. Acad. Sci. USA. 2001. V. 98. P. 9056-9061.Vargas R., Garza J., Dixon D.A., Hay B.P. // J. Am. Chem. Soc. 2000. V. 122. P. 4750-4755.Cuthbertson J.M., Bond P. J., Sansom M.S. // Biochemistry. 2006. V. 45. P. 14298-14310.Wagner G., Pardi A., Wuthrich K. // J. Am. Chem. Soc. 1983. V. 105. P. 5948-5949.