Skip to main content
NCBI home page
Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1980 Jul;77(7):3791–3795. doi: 10.1073/pnas.77.7.3791

A theoretical study of the structure of parathyroid hormone.

J E Zull, N B Lev
PMCID: PMC349712  PMID: 6933435

Abstract

Theoretical analysis of the tertiary and secondary structure of parathyroid hormone was conducted. By combining interpretations from this analysis with chemical data available in the literature, certain structural features of the hormone are consistently predicted. The proposed model for the hormone contains two domains dominated by hydrophobic clustering of critical residues within each domain and separated by an exposed linker region. In the prediction of two domains with a linker region, the model is similar to that proposed by Fiskin et al. [Fiskin, A.M., Cohn, D.M. & Peterson, G.S. (1977) J. Biol. Chem. 252, 8261-8268], but it differs significantly in other respects. The proposed structural features are apparent in the bovine, human, and porcine species of hormone.

Full text

PDF
3791

Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. Brewer H. B., Jr, Ronan R. Bovine parathyroid hormone: amino acid sequence. Proc Natl Acad Sci U S A. 1970 Dec;67(4):1862–1869. doi: 10.1073/pnas.67.4.1862. [DOI] [PMC free article] [PubMed] [Google Scholar]
  2. Bundi A., Andreatta R. H., Wüthrich K. Characterisation of a local structure in the synthetic parathyroid hormone fragment 1--34 by 1H nuclear-magnetic-resonance techniques. Eur J Biochem. 1978 Nov 2;91(1):201–208. doi: 10.1111/j.1432-1033.1978.tb20952.x. [DOI] [PubMed] [Google Scholar]
  3. Chou P. Y., Fasman G. D. Conformational parameters for amino acids in helical, beta-sheet, and random coil regions calculated from proteins. Biochemistry. 1974 Jan 15;13(2):211–222. doi: 10.1021/bi00699a001. [DOI] [PubMed] [Google Scholar]
  4. Chou P. Y., Fasman G. D. Prediction of the secondary structure of proteins from their amino acid sequence. Adv Enzymol Relat Areas Mol Biol. 1978;47:45–148. doi: 10.1002/9780470122921.ch2. [DOI] [PubMed] [Google Scholar]
  5. D'Amour P., Segre G. V., Roth S. I., Potts J. T., Jr Analysis of parathyroid hormone and its fragments in rat tissues: chemical identification and microscopical localization. J Clin Invest. 1979 Jan;63(1):89–98. doi: 10.1172/JCI109283. [DOI] [PMC free article] [PubMed] [Google Scholar]
  6. Fiskin A. M., Cohn D. V., Peterson G. S. A model for the structure of bovine parathormone derived by dark field electron microsocpy. J Biol Chem. 1977 Nov 25;252(22):8261–8268. [PubMed] [Google Scholar]
  7. Habener J. F., Potts J. T., Jr Cleavage-associated enhancement of an antigenic site in the biologically active NH2-terminal region of parathyroid hormone. Endocrinology. 1979 Jul;105(1):115–119. doi: 10.1210/endo-105-1-115. [DOI] [PubMed] [Google Scholar]
  8. Heath E., Chuang J., Botti R. E., Jr, Whiteley B., Zull J. E. Metabolism of tritiated parathyroid hormone by a kidney cortex plasma membrane preparation. J Biol Chem. 1980 Feb 25;255(4):1577–1585. [PubMed] [Google Scholar]
  9. Mahaffey J. E., Rosenblatt M., Shepard G. L., Potts J. T., Jr Parathyroid hormone inhibitors. Determination of minimum sequence requirements. J Biol Chem. 1979 Jul 25;254(14):6496–6498. [PubMed] [Google Scholar]
  10. Moews P. C., Knox J. R. Predicted secondary structures of four penicillin beta-lactamases and a comparison with two lysozymes. Int J Pept Protein Res. 1979 Apr;13(4):385–393. doi: 10.1111/j.1399-3011.1979.tb01897.x. [DOI] [PubMed] [Google Scholar]
  11. Nozaki Y., Tanford C. The solubility of amino acids and two glycine peptides in aqueous ethanol and dioxane solutions. Establishment of a hydrophobicity scale. J Biol Chem. 1971 Apr 10;246(7):2211–2217. [PubMed] [Google Scholar]
  12. Rose G. D. Prediction of chain turns in globular proteins on a hydrophobic basis. Nature. 1978 Apr 13;272(5654):586–590. doi: 10.1038/272586a0. [DOI] [PubMed] [Google Scholar]
  13. Rose G. D., Wetlaufer D. B. The number of turns in globular proteins. Nature. 1977 Aug 25;268(5622):769–770. doi: 10.1038/268769a0. [DOI] [PubMed] [Google Scholar]
  14. Rosenblatt M., Callahan E. N., Mahaffey J. E., Pont A., Potts J. T., Jr Parathyroid hormone inhibitors. Design, synthesis, and biologic evaluation of hormone analogues. J Biol Chem. 1977 Aug 25;252(16):5847–5851. [PubMed] [Google Scholar]
  15. Rosenblatt M., Goltzman D., Keutmann H. T., Tregear G. W., Potts J. T., Jr Chemical and biological properties of synthetic, sulfur-free analogues of parathyroid hormone. J Biol Chem. 1976 Jan 10;251(1):159–164. [PubMed] [Google Scholar]
  16. Rosenblatt M., Potts J. T., Jr Design and synthesis of parathyroid hormone analogues of enhanced biological activity. Endocr Res Commun. 1977;4(2):115–133. doi: 10.3109/07435807709073917. [DOI] [PubMed] [Google Scholar]
  17. Rottem S., Slutzky G. M., Bittman R. Cholesterol distribution and movement in the Mycoplasma gallisepticum cell membrane. Biochemistry. 1978 Jul 11;17(14):2723–2726. doi: 10.1021/bi00607a005. [DOI] [PubMed] [Google Scholar]
  18. Sauer R. T., Niall H. D., Hogan M. L., Keutmann H. T., O'Riordan J. L., Potts J. T., Jr The amino acid sequence of porcine parathyroid hormone. Biochemistry. 1974 Apr 23;13(9):1994–1999. doi: 10.1021/bi00706a033. [DOI] [PubMed] [Google Scholar]
  19. Schiffer M., Edmundson A. B. Use of helical wheels to represent the structures of proteins and to identify segments with helical potential. Biophys J. 1967 Mar;7(2):121–135. doi: 10.1016/S0006-3495(67)86579-2. [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Schiller P. W., Yam C. F., Lis M. Evidence for topographical analogy between methionine-enkephalin and morphine derivatives. Biochemistry. 1977 May 3;16(9):1831–1838. doi: 10.1021/bi00628a011. [DOI] [PubMed] [Google Scholar]
  21. TASHJIAN A. H., Jr, ONTJES D. A., MUNSON P. L. ALKYLATION AND OXIDATION OF METHIONINE IN BOVINE PARATHYROID HORMONE: EFFECTS ON HORMONAL ACTIVITY AND ANTIGENICITY. Biochemistry. 1964 Aug;3:1175–1182. doi: 10.1021/bi00896a029. [DOI] [PubMed] [Google Scholar]
  22. Tregear G. W., Van Rietschoten J., Greene E., Keutmann H. T., Niall H. D., Reit B., Parsons J. A., Potts J. T., Jr Bovine parathyroid hormone: minimum chain length of synthetic peptide required for biological activity. Endocrinology. 1973 Dec;93(6):1349–1353. doi: 10.1210/endo-93-6-1349. [DOI] [PubMed] [Google Scholar]
  23. Woodhead J. S., O'Riordan J. L., Keutmann H. T., Stoltz M. L., Dawson B. F., Niall H. D., Robinson C. J., Potts J. T., Jr Isolation and chemical properties of porcine parathyroid hormone. Biochemistry. 1971 Jul 6;10(14):2787–2792. doi: 10.1021/bi00790a021. [DOI] [PubMed] [Google Scholar]
  24. Zull J. E., Malbon C. C., Chuang J. Binding of tritiated bovine parathyroid hormone to plasma membranes from bovine kidney cortex. J Biol Chem. 1977 Feb 10;252(3):1071–1078. [PubMed] [Google Scholar]

Articles from Proceedings of the National Academy of Sciences of the United States of America are provided here courtesy of National Academy of Sciences

RESOURCES