The amphipathic helix: its possible role in the interaction of glucagon and other peptide hormones with membrane receptor sites
作者： Richard M. Epand
DOI: 10.1016/0968-0004(83)90212-8
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摘要: Abstract Structure-function studies of glucagon suggest that relatively non-specific hydrophobic interactions participate in the binding this hormone to cell surface receptors. These may occur as a result formation segments amphipatic helix peptide. This also endows with ability solubilize phospholipids manner which is similar solubilization by serum apolipoprotein A-1. Glucagon shares form amphipathic helices and interact several other polypeptide hormones bind receptor sites analogous mechanisms.
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sci-hub.se 参考文章(24)
R.M. Epand, G. Rosselin, D.H. Hoa, T.E. Cote, M. Laburthe, Structural requirements for glucagon receptor binding and activation of adenylate cyclase in liver. Study of chemically modified forms of the hormone, including N alpha-trinitrophenyl glucagon, an antagonist. Journal of Biological Chemistry. ,vol. 256, pp. 1128- 1132 ,(1981) , 10.1016/S0021-9258(19)69937-0
E A Carrey, R M Epand, The role of nonspecific hydrophobic interactions in the biological activity of N epsilon-acyl derivatives of glucagon. Studies of conformation, receptor binding, and adenylate cyclase activation. Journal of Biological Chemistry. ,vol. 257, pp. 10624- 10630 ,(1982) , 10.1016/S0021-9258(18)33868-7
R M Epand, J J Liepnieks, Conformational and biological properties of di[delta-(5-nitro-2-pyrimidyl)ornithine 17,18]glucagon. Role of the arginine residues. Journal of Biological Chemistry. ,vol. 258, pp. 203- 207 ,(1983) , 10.1016/S0021-9258(18)33241-1
D.E. Wright, M. Rodbell, Preparation of 2-thioltryptophan-glucagon and (tryptophan-S-glucagon)2. Differences in binding to the glucagon receptor in the hepatic adenylate cyclase system. Journal of Biological Chemistry. ,vol. 255, pp. 10884- 10887 ,(1980) , 10.1016/S0021-9258(19)70389-5
D.E. Wright, M. Rodbell, Glucagon1-6 binds to the glucagon receptor and activates hepatic adenylate cyclase. Journal of Biological Chemistry. ,vol. 254, pp. 268- 269 ,(1979) , 10.1016/S0021-9258(17)37911-5
Gerhard Wider, Kong Hung Lee, Kurt Wüthrich, Sequential resonance assignments in protein 1H nuclear magnetic resonance spectra. Glucagon bound to perdeuterated dodecylphosphocholine micelles. Journal of Molecular Biology. ,vol. 155, pp. 367- 388 ,(1982) , 10.1016/0022-2836(82)90010-9
M.D. Bregman, D. Trivedi, V.J. Hruby, Glucagon amino groups. Evaluation of modifications leading to antagonism and agonism Journal of Biological Chemistry. ,vol. 255, pp. 11725- 11731 ,(1980) , 10.1016/S0021-9258(19)70194-X
Tom Blundell, Conformation and molecular biology of polypeptide hormones II. Glucagon Trends in Biochemical Sciences. ,vol. 4, pp. 80- 83 ,(1979) , 10.1016/0968-0004(79)90187-7
Richard M. Epand, The apparent preferential interaction of human plasma high density apolipoprotein A-I with gel-state phospholipids Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism. ,vol. 712, pp. 146- 151 ,(1982) , 10.1016/0005-2760(82)90096-0
Michael C. Lin, Simonetta Nicosia, Martin Rodbell, Effects of iodination of tyrosyl residues on the binding and action of glucagon at its receptor Biochemistry. ,vol. 15, pp. 4537- 4540 ,(1976) , 10.1021/BI00665A031