Structures of ovine corticotropin-releasing factor and its Ala32 mutant as studied by CD and NMR techniques

Journal of Biochemistry

Volumn 127, Issue 4, 2000, Pages 687-694

  Ryu, Kyoung Seok ^a   Choi, Byong Seok ^a,b   Chi, Seung Wook ^a   Kim, Seung Ho ^a   Kim, Hyoungman ^a  

^a Korea Advanced Institute of Science and Technology (KAIST)   (South Korea)

^b Korea Research Institute of Bioscience and Biotechnology (KRIBB)   (South Korea)

Author keywords

CD; Chemical shift; Corticotropin releasing factor; NMR; Stability; helix

Indexed keywords

ALANINE; CORTICOTROPIN RELEASING FACTOR; MUTANT PROTEIN;

ALPHA HELIX; AMINO ACID SUBSTITUTION; ANIMAL CELL; ARTICLE; CIRCULAR DICHROISM; CORTICOTROPIN RELEASE; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PROTEIN CONFORMATION; PROTEIN STABILITY; PROTEIN STRUCTURE; SHEEP; STRUCTURE ANALYSIS;

ANIMALIA; OVIS; OVIS ARIES;

EID: 0034087720     PISSN: 0021924X     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.jbchem.a022658     Document Type: Article

References (45)

1. Vale, W., Spiess, J., Rivier, C., and Rivier, J. (1981) Characterizaion of a 41-residue ovine hypothalamic peptide that stimulates secretion of corticotropin and β-endorphin. Science 213, 1394-1397
2. Richard, D. (1992) Involvement of corticotropin-releasing factor in the control of food intake and energy expenditure. Ann. N. Y. Acad. Sci. 155-172
3. Menzaghi, F., Heinrichs, S.C., Pich, E.M., Weiss, F., and Koob, G.F. (1992) The role of limbic and hypothalamic corticotropin-releasing factor in behavioral respinses to stress. Ann. N. Y. Acad. Sci. 142-154
4. Dufau, M.L., Tinajero, J.C., and Fabbri, A. (1993) Corticotropin-releasing factor: an antireproductive hormone of the testis. FASEB J. 7, 299-307
5. Rivier, J., Rivier, C., and Vale, W. (1984) Synthetic competitive antagonists of corticotropin-releasing factor: Effect on ACTH secretion in the rat. Science 224, 889-891
6. Chalmers, D.T., Lovenbergand, T.W., and De Souza, E.B. (1995) Localization of novel corticotropin-releasing factor receptor (CRF2) mRNA expression to specific subcortical nuclei in rat brain: comparison with CRF1 receptor mRNA expression. J. Neurosci. 15, 6340-6350
7. Lovenberg, T.W., Chalmers, D.T., Liu, C., and De Souza, E.B. (1995) CRF2 alpha and CRF2 beta receptor mRNAs are differentially distributed between the rat central nervous system and peripheral tissues. Endocrinology 136, 4139-4142
8. Woods, R.J., Kennedy, K.M., Gibbins, J.M., Behan, D., Vale, W., and Lowry, P.J. (1994) Corticotropin-releasing factor binding protein dimerizes after association with ligand. Endocrinology 135, 768-773
9. Lowry, P.J., Koerber, S.C., Woods, R.J., Baigent, S., Sutton, S., Behan, D.P., Vale, W., and Rivier, J. (1996) Nature of ligand affinity and dimerization of corticotropin-releasing factor-binding protein may be detected by circular dichroism. J. Endocrinol. 16, 39-44
10. 1H NMR and distance geometry with restrained dynamics. Protein Eng. 6, 149-156
11. Kornreich, W.D., Galyean, R., Hernandez, J.-F., Craig, A.G., Donaldson, C.J., Yamamoto, G., Rivier, C., Vale, W., and Rivier, J. (1992) Alanine series of ovine corticotropin releasing factor (oCRF): A structure-activity relationship study. J. Med. Chem. 35, 1870-1876
12. O'Neil, K.T. and DeGrado, W.F. (1990) A thermodynamic scale for the helix-forming tendencies of the commonly occurring amino acids. Science 250, 646-651
13. Sonnichsen, F.D., Van Eyk, J.E., Hodges, R.S., and Sykes, B.D. (1992) Effect of trifluoroethanol on protein secondary structure: An NMR and CD study using a synthetic actin peptide. Biochemistry 31, 8790-8798
14. Walgers, R., Lee, T.C., and Cammers-Goodwin, A. (1998) An indirect chaotropic mechanism for the stabilization of helix conformation of peptides is aqueous trifluoroethanol and hexafluoro-2-propanol. J. Am. Chem. Soc. 120, 5073-5079
15. Jasanoff, A. and Fercht, A.R. (1994) Quantitative determination of helical protensities from trifluoroethanol titration curves. Biochemistry 33, 2129-2135
16. Motta, A., Pastore, A., Goud, N.A., and Castiglione Morelli, M.A. (1991) Solution conformation of salmon calcitonin in sodium dodecyl sulfate micelles as determined by two-dimensional NMR and distance geometry calculations. Biochemistry 30, 10444-10450
17. Mukhopadhyay, K. and Basak, S. (1998) Conformation induction in melanotropic peptides by trifluoroethanol: fluorescence and circular dichroism study. Biophys. Chem. 74, 175-186
18. Wishart, D.S. and Sykes, B.D. (1994) Chemical shifts as a tool for structure determination in Methods in Enzymology (James, T.L. and Oppenheimer, N.J., eds.) Vol. 239, pp. 363-439, Academic Press, New York
19. Wishart, S., Sykes, B.D., and Richards, F.M. (1992) The chemical shift index: A fast and simple method for the assignment of protein secondary structure through NMR spectroscopy. Biochemistry 31, 1647-1651
20. 1H NMR assignments and secondary structure identification of human ubiquitin. Biochemistry 26, 7282-7290
21. 1H NMR chemical shifts in proteins. J. Am. Chem. Soc. 105, 5948-5949
22. Blanco, F.J., Herranz, J., González, C., Jiménez, M.A., Rico, M., Santoro, J., and Nieto, J.L. (1992) NMR chemical shifts: A tool to characterize distortions of peptide and protein helices. J. Am. Chem. Soc. 114, 9676-9677
23. Holtzer, M.E. and Holtzer, A. (1992) α-Helix to random coil transition: Determination of peptide concentration from the CD at the isodichroic point. Biopolymers 32, 1675-1677
24. Udenfriend, S., Stein, S., Bohlen, P., and Dairman, W. (1972) Fluorescamine: A reagent for assay of amino acids, peptides, proteins, and primary amines in the picomole range. Science 178, 871-872
25. Peterson, G.L. (1983) Determination of total protein in Methods in Enzymology (Hirs, C.H.W. and Timasheff, S.N., eds.) Vol. 91, pp. 95-121, Academic Press, New York
26. Pallai, P.V., Mabilia, M., Goodman, M., Vale, W., and Rivier, J. (1983) Structural homology of corticotropin-releasing factor, sauvagine, and urotensin I: circular dichroism and prediction studies. Proc. Natl. Acad. Sci. USA 80, 6770-6774
27. Merutka, G. and Stellwagen, E. (1989) Analysis of peptides for helical prediction. Biochemistry 28, 352-357
28. Lau, S.H., Rivier, J., Vale, W., Kaiser, E.T., and Kézdy, F.J. (1983) Surface properties of an amphiphilic peptide hormone and of its analog: Corticotropin-releasing factor and sauvagine. Proc. Natl. Acad. Sci. USA 80, 7070-7074
29. Morii, H., Uedaira, H., Ishimura, M., Kidokoro, S.-I., Kokubu, T., and Ohashi, S. (1997) Special folding pathway to tetramer only through the micelle state of the corticotropin-releasing factor. Biochemistry 36, 15538-15545
30. Zhou, N.B., Zhu, B.-Y., Kay, C.M., and Hodges, R.S. (1992) The two-stranded α-helical coiled-coil is an ideal model for studying protein stability and subunit interactions. Biopolymers 32, 419-426
31. Luo, P. and Baldwin, R.L. (1997) Mechanism of helix induction by trifluoroethanol: A framework for extrapolating the helix-forming properties of peptides from trifluoroethanol/water mixtures back to water. Biochemistry 36, 8413-8421
32. Chen, Y.H. and Yang, J.T. (1971) A new approach to the calculation of secondary structure of globular proteins by optical rotatory dispersion and circular dichroism. Biochem. Biophys. Res. Commun. 44, 1285-1291
33. Chen, Y.H., Yang, J.T., and Chau, K.H. (1974) Determination of the helix and β form of proteins in aqueous solution by circular dichroism. Biochemistry 13, 3350-3359
34. 13C-labeled proteins. J. Magn. Reson. 91, 84-92
35. Hill, J.M., Oomen, C.J., Miranda, L.P., Binghan, J.-P., Alewood, P.F., and Craik, D.J. (1998) Three-dimensional solution structure of α-conotoxin MII by NMR spectroscopy: Effects of solution environment on helicity. Biochemistry 37, 15621-15630
36. Hoyt, D.W. and Gierasch, L.M. (1991) Hydrophobic content and lipid interactions of wild-type and mutant OmpA signal peptides correlate with their in vivo function. Biochemistry 30, 10155-10163
37. Lazo, N.D. and Downing, D.T. (1997) Circular dichroism of model peptides emulating the amphipathic alpha-helical regions of intermediate filaments. Biochemistry 36, 2559-2565
38. Zhou, N.E., Zhu, B.-Y., Sykes, B.D., and Hodges, R.S. (1992) Relationship between amide proton chemical shifts and hydrogen bonding in amphipathic α-helical peptides. J. Am. Chem. Soc. 114, 4320-4326
39. Koerber, S.C., Gulyas, J., Lahrichi, S.L., Corrigan, A., Craig, A.G., Rivier, C., Vale, W., and Rivier, J. (1998) Constrained corticotropin-releasing factor (CRF) agonists and antagonists with i - (i + 3) Glu-Xaa-DXbb-Lys bridges. J. Med. Chem. 41, 5002-5011
40. Armstrong, K.M. and Baldwin, R.L. (1993) Charged histidine affects alpha-helix stability at all positions in the helix by interacting with the backbone charges. Proc. Natl. Acad. Sci. USA 90, 11337-11340
41. Zimm, B.H. and Bragg, J.K. (1959) Theroy of the phase transition between helix and random coil in polypeptide chains. J. Chem. Phys. 31, 526-535
42. Lifson, S. and Roig, A. (1961) On the theory of helix-coil transition in polypeptides. J. Chem. Phys. 34, 1963-1974
43. Gulyas, J., Rivier, C., Perrin, M., Koerber, S.C., Sutton, S., Corringan, A., Lahrichi, S.L., Craig, A.G., Vale, W., and Rivier, J. (1995) Potent, structurally constrained agonists and competitive antagonists of corticotropin-releasing factor. Proc. Natl. Acad. Sci. USA 92, 10575-10579
44. van der Goot, F.G., Gonzalez-Manas, J.M., Lakey, J.H., and Pattus, F. (1991) A molten-globule membrane-insertion intermediate of the pore-forming domain of colicin A. Nature 354, 408-410
45. Fernandez, M.S. (1981) Determination of surface potential in liposomes. Biochim. Biophys. Acta 6, 23-26