Skip to main content
SpringerLink
Log in

Structural basis of protein–protein interaction studied by NMR

  • Original Paper
  • Published:
Journal of Structural and Functional Genomics

Abstract

This paper describes efforts of the structural genomics project in the nuclear magnetic resonance (NMR) laboratory at the University of Science and Technology of China. This structural genomics project is biological-functional driven. Targets are mainly selected from two systems: proteins related with regulation of gene expression in humans and other eukaryotes, and proteins existing in the cell junction in humans. The majority of proteins selected from these two systems are related with human health and diseases, and some are potential drug targets. Twenty-five protein structures from Homo sapiens and other eukaryotes have been determined during last 5 years in this laboratory. Nuclear magnetic resonance (NMR) spectroscopy is highly suited to investigate molecular interactions at a close physiological condition and is particularly suited for the study of low-affinity, transient complexes. It can provide information on protein surface interaction, their complex structure, and their dynamic properties during protein recognition. Several examples are given in this paper.

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

Access this article

Log in via an institution

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

Instant access to the full article PDF.

Institutional subscriptions

Similar content being viewed by others

References

  1. Bonvin AM, Boelens R, Kaptein R (2005) Curr Opin Chem Biol 9:501–508

    Article  PubMed  CAS  Google Scholar 

  2. Chen Q, Niu X, Xu Y, Wu J, Shi Y (2007) Protein Sci 16:1053–1062

    Article  PubMed  CAS  Google Scholar 

  3. Dai H, Huang W, Xu J, Yao B, Xiong S, Ding H, Tang Y, Liu H, Wu J, Shi Y (2006) Biochim Biophys Acta 1764:1688–1700

    PubMed  CAS  Google Scholar 

  4. Dejana E (2004) Nat Rev Mol Cell Biol 5:261–270

    Article  PubMed  CAS  Google Scholar 

  5. Ding H, Xu Y, Chen Q, Dai H, Tang Y, Wu J, Shi Y (2005a) Biochemistry 44:2790–2799

    Article  PubMed  CAS  Google Scholar 

  6. Ding H, Yang Y, Zhang J, Wu J, Liu H, Shi Y (2005b) Proteins 61:1050–1058

    Article  PubMed  CAS  Google Scholar 

  7. Dominguez C, Boelens R, Bonvin AM (2003) J Am Chem Soc 125:1731–1737

    Article  PubMed  CAS  Google Scholar 

  8. Fu H (2004) Protein-protein interactions: methods and applications. Humana Press, Totowa

    Google Scholar 

  9. Golemis E (2002) Protein-protein interactions: a molecular cloning manual. Cold Spring Harbor Laboratory Press, Cold Spring Harbor

    Google Scholar 

  10. Hunt I (2005) Protein Expr Purif 40:1–22

    Article  PubMed  CAS  Google Scholar 

  11. Juneja J, Udgaonkar JB (2003) Curr Sci 84:157–172

    CAS  Google Scholar 

  12. Kourlas PJ, Strout MP, Becknell B, Veronese ML, Croce CM, Theil KS, Krahe R, Ruutu T, Knuutila S, Bloomfield CD et al (2000) Proc Natl Acad Sci USA 97:2145–2150

    Article  PubMed  CAS  Google Scholar 

  13. Li X, Zhang J, Cao Z, Wu J, Shi Y (2006) Protein Sci 15:2149–2158

    Article  PubMed  CAS  Google Scholar 

  14. Matter K, Balda MS (2003) Nat Rev Mol Cell Biol 4:225–236

    Article  PubMed  CAS  Google Scholar 

  15. Orphanides G, Reinberg D (2002) Cell 108:439–451

    Article  PubMed  CAS  Google Scholar 

  16. Pawson T, Nash P (2003) Science 300:445–452

    Article  PubMed  CAS  Google Scholar 

  17. Pellecchia M, Sem DS, Wuthrich K (2002) Nat Rev Drug Discov 1:211–219

    Article  PubMed  CAS  Google Scholar 

  18. Peng C, Liu H, Zhou M, Zhang L, Li X, Shen S, Li G (2007) Mol Cell Biochem 303:141–149

    Article  PubMed  CAS  Google Scholar 

  19. Pickford AR, Campbell ID (2004) Chem Rev 104:3557–3566

    Article  PubMed  CAS  Google Scholar 

  20. Prasad R, Gu Y, Alder H, Nakamura T, Canaani O, Saito H, Huebner K, Gale RP, Nowell PC, Kuriyama K et al (1993) Cancer Res 53:5624–5628

    PubMed  CAS  Google Scholar 

  21. Reisman DN, Sciarrotta J, Wang W, Funkhouser WK, Weissman BE (2003) Cancer Res 63:560–566

    PubMed  CAS  Google Scholar 

  22. Sauer U, Lasko DR, Fiaux J, Hochuli M, Glaser R, Szyperski T, Wuthrich K, Bailey JE (1999) J Bacteriol 181:6679–6688

    PubMed  CAS  Google Scholar 

  23. Shen W, Xu C, Huang W, Zhang J, Carlson JE, Tu X, Wu J, Shi Y (2007) Biochemistry 46:2100–2110

    Article  PubMed  CAS  Google Scholar 

  24. Stamatoyannopoulos G (2001) The molecular basis of blood diseases, 3rd edn. W.B. Saunders, Philadelphia

    Google Scholar 

  25. Sun J, Zhang J, Wu F, Xu C, Li S, Zhao W, Wu Z, Wu J, Zhou CZ, Shi Y (2005) Biochemistry 44:8801–8809

    Article  PubMed  CAS  Google Scholar 

  26. Sun H, Dai H, Zhang J, Jin X, Xiong S, Xu J, Wu J, Shi Y (2006) J Biomol NMR 36:295–300

    Article  PubMed  CAS  Google Scholar 

  27. Vaynberg J, Qin J (2006) Trends Biotechnol 24:22–27

    Article  PubMed  CAS  Google Scholar 

  28. Vignali M, Hassan AH, Neely KE, Workman JL (2000) Mol Cell Biol 20:1899–1910

    Article  PubMed  CAS  Google Scholar 

  29. Wong AK, Shanahan F, Chen Y, Lian L, Ha P, Hendricks K, Ghaffari S, Iliev D, Penn B, Woodland AM et al (2000) Cancer Res 60:6171–6177

    PubMed  CAS  Google Scholar 

  30. Xu Y, Yang W, Wu J, Shi Y (2002) Biochemistry 41:5415–5420

    Article  PubMed  CAS  Google Scholar 

  31. Xu C, Zheng P, Shen S, Xu Y, Wei L, Gao H, Wang S, Zhu C, Tang Y, Wu J et al (2005) FEBS Lett 579:2788–2794

    Article  PubMed  CAS  Google Scholar 

  32. Xu C, Zhang J, Huang X, Sun J, Xu Y, Tang Y, Wu J, Shi Y, Huang Q, Zhang Q. (2006a) J Biol Chem 281:15900–15908

    Article  PubMed  CAS  Google Scholar 

  33. Xu J, Zhang J, Wang L, Zhou J, Huang H, Wu J, Zhong Y, Shi Y. (2006b) Proc Natl Acad Sci USA 103:11625–11630

    Article  PubMed  CAS  Google Scholar 

  34. Yang W, Xu Y, Wu J, Zeng W, Shi Y (2003) Biochemistry 42:1930–1938

    Article  PubMed  CAS  Google Scholar 

  35. Yao B, Zhang J, Dai H, Sun J, Jiao Y, Tang Y, Wu J, Shi Y (2007) Biochim Biophys Acta 1774:35–43

    PubMed  CAS  Google Scholar 

  36. Yee A, Gutmanas A, Arrowsmith CH (2006) Curr Opin Struct Biol 16:611–617

    Article  PubMed  CAS  Google Scholar 

  37. Zhou H, Xu Y, Yang Y, Huang A, Wu J, Shi Y (2005) J Biol Chem 280:13841–13847

    Google Scholar 

Download references

Acknowledgements

This work was supported by the Chinese National Fundamental Research Project (Grant 2002CB713806, 2006CB806507 and 2006CB910201), the Chinese National Natural Science Foundation (Grant 30121001, 30570361 and 30670426), the Key Project of the National High Technology Research and Development Program of China (Grant 2002BA711A13), and the Pilot Project of the Knowledge Innovation Program of the Chinese Academy of Science (Grant KSCX1-SW-17). The authors would like to thank Jiahai Zhang, Chunlei Pu, and Yajun Tang for technical support and thank graduate students who contributed to the work.

Author information

Authors and Affiliations

  1. Hefei National Laboratory for Physical Sciences at Microscale and School of Life Sciences, University of Science and Technology of China, Hefei, Anhui, 230026, People’s Republic of China

    Yunyu Shi & Jihui Wu

Authors
  1. Yunyu Shi
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Jihui Wu
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Yunyu Shi.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Shi, Y., Wu, J. Structural basis of protein–protein interaction studied by NMR. J Struct Funct Genomics 8, 67–72 (2007). https://doi.org/10.1007/s10969-007-9021-8

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s10969-007-9021-8

Keywords

Search

Navigation