Abstract
In humans, two endothelin receptors, ETa and ETb, are activated by three endogenous 21-mer cyclic peptides, ET-1, ET-2, and ET-3, which control various physiological processes, including vasoconstriction, vasodilation, and stimulation of cell proliferation. The first stage of this study it to produce a stable solubilized and purified receptor in a monodisperse state. This article is focused on the engineering, expression, purification, and characterization of the endothelin receptor B for subsequent structural and functional studies.
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References
Barton, M. and Yanagisawa, M., Endothelin: 20 years from discovery to therapy, Can. J. Physiol. Pharmacol., 2008, vol. 86, pp. 485–498.
Haendler, B., Hechler, U., and Schleuning, W.-D., Molecular cloning of human endothelin (ET) receptors ETA and ETB, J. Cardiovasc. Pharmacol., 1992, vol. 20, pp. 1–4.
Davenport, A.P., D’Orleans-Juste, P., Godfraind, Th., Maguire, J.J., Ohlstein, E.H., and Ruffolo, R.R., Endothelin receptors: ETB receptor. IUPHAR Database (IUPHAR-DB.ORG). Last modified on May 23, 2014; accessed on July 19, 2014.
Kohan, D.E., Cleland, J.G., Rubin, L.J., Theodorescu, D., and Barton, M., Clinical trials with endothelin receptor antagonists: what went wrong and where can we improve?, Life Sci., 2012, vol. 91, pp. 528–539.
Katritch, V., Cherezov, V., and Stevens, R.C., Structure-function of the g protein-coupled receptor superfamily, Annu. Rev. Pharmacol. Toxicol., 2013, vol. 53, pp. 531–556.
Zhou, X.E., Melcher, K., and Xu, H.E., Structure and activation of rhodopsin, Acta Pharmacol. Sinica, 2012, vol. 33, pp. 291–299.
Rosenbaum, D.M., Cherezov, V., Hanson, M.A., Rasmussen, S.G., Thian, F.S., Kobilka, T.S., Choi, H.J., Yao, X.J., Weis, W.I., Stevens, R.C., and Kobilka, B.K., GPCR engineering yields high-resolution structural insights into beta2-adrenergic receptor function, Science, 2007, vol. 318, pp. 1266–1273.
Liu, W., Chun, E., Thompson, A.A., Chubukov, P., Xu, F., Katritch, V., Han, G.W., Roth, C.B., Heitman, L.H., Izerman, A.P., Cherezov, V., and Stevens, R.C., Structural basis for allosteric regulation of GPCRs by sodium ions, Science, 2012, vol. 337, pp. 232–236.
Maeda, S. and Schertler, G., Production of GPCR and GPCR complexes for structure determination, Curr. Opin. Sctruct. Biol., 2013, vol. 23, no. 3, pp. 381–392.
Seddon, A.M., Curnow, P., and Booth, P.J., Membrane proteins, lipids and detergents: not just a soap opera, Biochim. Biophys. Acta., 2004, vol. 1666, nos. 1/2, pp. 105–117.
Thompson, A.A., Liu, J.J., Chun, E., Wacker, D., Wu, H., Cherezov, V., and Stevens, R.C., GPCR stabilization using the bicelle-like architecture of mixed sterol-detergent micelles, Methods, 2011, vol. 55, pp. 310–317.
Joseph J.S., Abola E.E., and Cherezov V., in Cholesterol Regulation of Ion Channels and Receptors, London: Wiley, 2012, Ch. 11, pp. 231–253.
Deupi, X., Li, X.-D., and Schertler, G.F.X., Ligands stabilize specific GPCR conformations: but how?, Structure, 2012, vol. 2, Iss. 8, pp. 1289–1290.
Wu, H., Wacker, D., Mileni, M., Katritch, V., Han, G.W., Vardy, E., Liu, W., Thompson, A.A., Huang, X.-P., Carroll, F.I., Mascarella, S.W., Westkaemper, R.B., Mosier, P.D., Roth, B.L., Cherezov, V., and Stevens, R.C., Structure of the human k-opioid receptor in complex with JDTic, Nature, 2012, vol. 485, pp. 327–332.
Alexandrov, A.I., Mileni, M., Chien, E.Y., Hanson, M.A., and Stevens, R.C., Microscale fluorescent thermal stability assay for membrane proteins, Structure, 2008, vol. 16, pp. 351–359.
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Original Russian Text © A.V. Mishin, A.P. Luginina, A.P. Potapenko, V.I. Borshchevskiy, V. Katritch, E. Edelweiss, I.S. Okhrimenko, V.I. Gordeliy, V.G. Cherezov, 2016, published in Doklady Akademii Nauk, 2016, Vol. 467, No. 6, pp. 725–729.
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Mishin, A.V., Luginina, A.P., Potapenko, A.P. et al. Expression and purification of an engineered human endothelin receptor B in a monomeric form. Dokl Biochem Biophys 467, 157–161 (2016). https://doi.org/10.1134/S1607672916020216
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DOI: https://doi.org/10.1134/S1607672916020216