Skip to main content
Log in

Structural analysis of desheptapeptide(B24-B30) insulin by molecular replacement

  • Published:
Science in China Series C: Life Sciences Aims and scope Submit manuscript

Abstract

Desheptapeptide (B24-B30) insulin (DHPI), a virtually inactive insulin analog, has been crystallized in space group P2, 2, 2, with two DHPI molecules in an asymmetric unit. The orientatin and positions of the molecules were determind by molecular replacement. and a structural model was built at 0.3 nm resolution. The current model shows that the two DMHI monomers are related by a non-crystallographic 2-fold axis, nearly parallel to the crystallographicc axis. This structural feature complicated the determination of the orientation of the local 2-fold axis, which was later confirmed by analysing the diffraction data of DHPI crystals.

This is a preview of subscription content, log in via an institution to check access.

Access this article

Price excludes VAT (USA)
Tax calculation will be finalised during checkout.

Instant access to the full article PDF.

Similar content being viewed by others

References

  1. Tager, H., Thomas, N., Assian, R. et al., Semisynthesis and biological activity of porcine[LeuB24] insulin and [LeuB25] insulin,Proc. Natl. Atad. Sci. USA, 1980, 77:3I81.

    Google Scholar 

  2. Shoelson, S., Haneda, M., Blix, P., et al., Three mutant insulins in man,Noture, 1983, 302: 540.

    Article  CAS  Google Scholar 

  3. Zhu, S. Q.,Molecular Architecture of Protein and Enzyme (eds. Bradshaw, R.A., Tang, J.), New York: Academic Press, Inc., 1985. 185–197.

    Google Scholar 

  4. Liang, D. C., Chang, W. R., Zhang, J. P. et al., The possible mechanism of binding interaction of insulin mo1ecule with its receptor,Science in China. Ser. B, 1992, 35: 547.

    CAS  Google Scholar 

  5. Spoden, M., Gatiner, H, G., Zahn, H. et al., Structure-function relationship ot des (B26-B30) insulin,Int. J. Peptide Prvtein Res., 1995, 46: 221.

    CAS  Google Scholar 

  6. Navaza, J., AMoRe: an automated package for molecular replacement,Acta Cryst., 1994, A50:157

    CAS  Google Scholar 

  7. Chang, W. R., Xie, D. L., Liang, D. C. et al., Crystallographic studies on deheptepeptide (B24-B30) insulin. Sci. Sin., Ser. B, 1982, 25: 385.

    CAS  Google Scholar 

  8. Nonh, A. C. T., Philips, D. C., Mathews, F. S., A semi-emphirical method of absorption correction,Acta Cryst., 1968, A24:351.

    Google Scholar 

  9. Collaborative Computational Project Nu. 4, The CCP4 suire:program for protein crystallography,Acta Cryst., 1994, D50: 760.

  10. Dai, J. B., Lou, M. Z., You, J. M. et al., Refinement of the structure of despentapeptide (B26-30) insulin at 0.15 nm resollution,Science in China, Ser B, 1987, 30(1): 54.

    Google Scholar 

  11. Hirshfeld, F.L., Symmetry in the generation of trial structures,Acta Cryst., 1968, 24:301.

    Article  Google Scholar 

  12. Hendrickson, W. A., Stereochemicnlly restrained refinement of macromolecular structures,Meth, Enzym., 1985, 115: 252.

    Article  CAS  Google Scholar 

  13. Roussel, A., Cambillau, C., TURBO-FRODO, inSilicon Graphics Geometry Partner Directory, California: Silicon Graphics, 1989, 77–78.

    Google Scholar 

Download references

Author information

Authors and Affiliations

Authors

Additional information

Project supported by the National Natural Science Foundation of China (Grant No. 39270156) and the Chinese Academy of Sciences.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Bao, S., Xie, D., Zhang, J. et al. Structural analysis of desheptapeptide(B24-B30) insulin by molecular replacement. Sci. China Ser. C.-Life Sci. 41, 258–264 (1998). https://doi.org/10.1007/BF02895100

Download citation

  • Received:

  • Issue Date:

  • DOI: https://doi.org/10.1007/BF02895100

Keywords

Navigation