Contribution of the absolutely conserved B8Gly to the foldability of insulin

Biological Chemistry

Volumn 384, Issue 5, 2003, Pages 805-809

  Gou, Zhan Yun ^a   Tang, Yue Hua ^a   Wang, Shuai ^a   Feng, You Min ^a  

^a INSTITUTE OF BIOCHEMISTRY AND CELL BIOLOGY   (China)

Author keywords

Disulfide; Foldability; Insulin; Refolding; Stability

Indexed keywords

ALANINE; AMINO ACID; DISULFIDE; GLYCINE; INSULIN; INSULIN DERIVATIVE; MUTANT PROTEIN;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; CONTROLLED STUDY; GENETIC CONSERVATION; IN VITRO STUDY; INSULIN RELEASE; MOLECULAR STABILITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; SEQUENCE ANALYSIS; STRUCTURE ANALYSIS; WILD TYPE;

ALANINE; AMINO ACID SUBSTITUTION; CIRCULAR DICHROISM; DISULFIDES; GLYCINE; GUANIDINE; INSULIN; PROTEIN FOLDING; RECOMBINANT PROTEINS; SACCHAROMYCES CEREVISIAE;

EID: 0038208331     PISSN: 14316730     EISSN: None     Source Type: Journal    
DOI: 10.1515/BC.2003.089     Document Type: Article

References (21)

1. Anfinsen, C.B. (1973). Principles that govern the folding of protein chains. Science 181, 223-230.
2. Baker, E.N., Blundell, T.L., Cutfield, J.F., Cutfield, S.M., Dodson, E.J., Dodson, G.G., Hodgkin, D.M.C., Hubbard, R.E., Isaacs, N.W., Reynolds, C.D. et al. (1988). The structure of 2Zn pig insulin crystals at 1.5 Å resolution. Phil. Trans. R. Soc. (London) B319, 369-456.
3. Chen, H. and Feng, Y.-M. (2001). Contribution of the residue Glu9, Glu46, and Phe49 to the biological activity of insulin-like growth factor 1. IUBMB Life 51, 33-37.
4. Derewenda, U., Derewenda, Z., Dodson, E.J., Dodson, G.G., Bing, X.G. and Markussen, J. (1991). X-ray analysis of the single chain B29-A1 peptide-linked insulin molecule. A completely inactive analogue. J. Mol. Biol. 220, 425-433.
5. Ellgaard, L., Molinari, M. and Helennius, A. (1999). Setting the standards: quality control in the secretory pathway. Science 286, 1882-1888.
6. Guo, Z.-Y. and Feng, Y.-M. (2001). Effects of cysteine to serine substitutions in the two inter-chain disulfide bonds of insulin. Biol. Chem. 382, 443-448.
7. Guo, Z.-Y., Shen, L. and Feng, Y.-M. (2002). The different folding behavior of insulln and insulin-like growth factor 1 is mainly controlled by their B-chain/domain. Biochemistry 41, 1556-1567.
8. Hua, Q.-X., Hu, S.-Q, Jia, W., Chu, Y.-C., Burke, G.T, Wang, S.H., Wang, R.-Y., Katsoyannis, P.G. and Weiss, M.A. (1998). Mini-proinsulin and mini-IGF-1: homologous protein sequences encoding non-homologous structures. J. Mol. Biol. 277, 103-118.
9. Hua, Q.X., Nakagawa, S.H., Jia, W., Hu, S.-Q., Chu, Y.-C., Katsoyannis, P.G. and Weiss, M.A. (2001). Hierarchical protein folding: asymmetric unfolding of an insulin analogue lacking the A7-B7 interchain disulfide bridge. Biochemistry 40, 12299-12311.
10. Konig, W. (1993). Peptide and Hormones: Structure, Regulation, Activity: A Reference Manual (Weinheim, Germany: Verlag Chemie).
11. Kristensen, C., Kjeldsen, T., Wiberg, F.C., Schaffer, L., Hach, M., Havelund, S., Bass, J., Steiner, D.F. and Andersen, A.S. (1997). Alanine mutagenesis of insulin. J. Biol. Chem. 272, 12978-12983.
12. Markussen, J., Dier, J., Engesgaard, A., Hansen, M.T., Hougaard, R, Langkjaer, L., Norris, K., Ribel, U., Sorensen, A.R., Sorensen, E. et al. (1987). Soluble, prolonged-acting insulin derivatives. II. Degree of protraction and crystallizability of insulins substituted in positions A17, B8, B13, B27 and B30. Protein Eng. 1, 215-223.
13. Nakagawa, S.H., Zhao, M., Hua, Q.-X. and Weiss, M.A. (1997). The importance of residue B8 in insulin activity, structure and folding. In: Peptides: Proceedings of the 15th American Peptide Symposium, J.P. Tam and P.T.P. Kaumaya, eds. (Amsterdam, The Netherlands: Kluwer/Escom), pp. 471-472.
14. Qiao, Z.-S., Guo, Z.-Y. and Feng, Y.-M. (2001). Putative disulfide-forming pathway of porcine insulin precursor during its refolding in vitro. Biochemistry 40, 2662-2668.
15. 1H NMR spectrum of the native human insulin monomer. Evidence for conformational differences between the monomer and aggregated forms. J. Biol. Chem. 265, 5448-5453.
16. Wang, C.C. and Tsou, C.L. (1991). The insulin A and B chains contain sufficient structural information to form the native molecule. Trends Biochem. Sci. 16, 279-281.
17. 13C labeling with application to protein design. Biochemistry 30, 7373-7389.
18. Weiss, M.A., Hua, QX, Jia, W., Chu, YC., Wang, R.Y and Katsoyannis, P.G. (2000). Hierarchical protein 'un-design': insulin's intrachain disulfide bridge tethers a recognition α-helix. Biochemistry 39, 15429-15440.
19. Zhang, H., Tang, Y.-H. and Feng, Y.-M. (2000). Possible role of B8GIy in insulin structural motif. Acta Biochim. Biophys. Sinica 32, 480-484.
20. Zhang, Y.-S., Hu, H.-M., Cai, R.-R., Feng, Y.-M., Zhu, S.-Q., He, Q.-B., Tang, Y.-H., Xu, M.-H., Xu, Y.-G., Liu, B. et al. (1996). Secretary expression of a single-chain insulin precursor in yeast and its conversion into human insulin. Sci. China (Series C) 39, 225-233.
21. Zhao, M., Nakagawa, S.H., Hua, Q.-X. and Weiss, M.A. (1997). Exploring the foldability of insulin by combinatorial chemistry. In: Peptides: Proceedings of the 15th American Peptide Symposium, J.P. Tam and P.T.P. Kaumaya, eds. (Amsterdam, The Netherlands: Kluwer/Escom), pp. 369-371.