Skip to main content
Log in

1H, 13C and 15N resonance assignments for the human E2 conjugating enzyme, UbcH7

  • Article
  • Published:
Biomolecular NMR Assignments Aims and scope Submit manuscript

Abstract

UbcH7 is a human E2 conjugating enzyme in the ubiquitin-dependent protein degradation pathway. The resonance assignments of UbcH7 will assist in elucidating the structural basis of interactions that occur within ubiquitination.

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.

Fig. 1

Similar content being viewed by others

Abbreviations

RING:

Really interesting new gene

HHARI:

Human homologue of Drosophila ariadne

NMR:

Nuclear magnetic resonance

HSQC:

Heteronuclear single quantum correlation

References

  • Ardley HC, Tan NG, Rose SA, Markham AF, Robinson PA (2001) Features of the parkin/ariadne-like ubiquitin ligase, HHARI, that regulate its interaction with the ubiquitin-conjugating enzyme, UbcH7. J Biol Chem 276:19640–19647

    Article  Google Scholar 

  • Delaglio F, Grzesiek S, Vuister GW, Zhu G, Pfeifer J, Bax A (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes. J Biomol NMR 6:277–293

    Article  Google Scholar 

  • Grzesiek S, Bax A (1992) An efficient experiment for sequential backbone assignment of medium-sized isotopically enriched proteins. J Magn Reson 99:201–207

    Google Scholar 

  • Hershko A, Ciechanover A (1998) The ubiquitin system. Annu Rev Biochem 67:425–479

    Article  Google Scholar 

  • Jentsch S (1992) The ubiquitin-conjugation system. Annu Rev Genet 26:177–205

    Article  Google Scholar 

  • Johnson BA, Blevins RA (1994) NMRView: a computer program for the visualization and analysis of NMR data. J Biomol NMR 4:603–614

    Article  Google Scholar 

  • Kay LE, Keifer P, Saarinen T (1992) Pure absorption gradient enhanced heteronuclear single quantum correlation spectroscopy with improved sensitivity. J Am Chem Soc 114:10663–10665

    Article  Google Scholar 

  • Kay LE, Xu G, Singer AU, Muhandiram DR, Forman-Kay JD (1993) A gradient-enhanced HCCH-TOCSY experiment for recording side-chain 1H and 13C correlations in H2O samples of proteins. J Magn Reson 101:333–337

    Article  Google Scholar 

  • Schubert M, Oschkinat H, Schmieder P (2001) MUSIC, selective pulses, and tuned delays: amino acid type-selective 1H–15N correlations, II. J Magn Reson 148:61–72

    Article  ADS  Google Scholar 

  • Zheng N, Wang P, Jeffrey PD, Pavletich NP (2000) Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases. Cell 102:533–539

    Article  Google Scholar 

Download references

Acknowledgments

The authors wish to thank Dr. Phillip Robinson and Dr. Helen Ardley for the UbcH7 plasmid. We would also like to thank Kathryn Barber for her technical support and Dr. Matthew Revington for his assistance in NMR data processing. This work was supported by grants from the Canadian Institutes of Health Research (CIHR), the Canada Research Chairs Program (G.S.S.), the CIHR Canada Graduate Scholarship (S.A.S.) and the Ontario Graduate Scholarship (S.A.S.).

Author information

Authors and Affiliations

Authors

Corresponding author

Correspondence to Gary S. Shaw.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Serniwka, S.A., Shaw, G.S. 1H, 13C and 15N resonance assignments for the human E2 conjugating enzyme, UbcH7. Biomol NMR Assign 2, 21–23 (2008). https://doi.org/10.1007/s12104-007-9074-4

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s12104-007-9074-4

Keywords

Navigation