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Biomolecular NMR Assignments

, Volume 1, Issue 1, pp 95–97 | Cite as

Backbone and sidechain 1H, 13C and 15N resonance assignments of the RGS domain from human RGS14

  • Elizabeth F. Dowler
  • Annette Diehl
  • Peter Schmieder
  • Christoph Brockmann
  • Jonathan Elkins
  • Meera Soundararajan
  • Hartmut Oschkinat
  • Linda J. Ball
Article
  • 60 Downloads

Abstract

We have assigned 1H, 15N and 13C resonances of the RGS domain from the human RGS14 protein, a multi-domain member of the RGS (Regulators of G-protein signalling) family of proteins, important in the down-regulation of specific G-protein signalling pathways.

Keywords

Chemical shift Regulator of G-protein signalling NMR RGS domain GTPase 

Abbreviations

RGS

Regulator of G-protein signaling

NaPi

Sodium phosphate buffer

IPTG

Isopropyl-beta-D-thiogalactopyranoside

Notes

Acknowledgements

The Structural Genomics Consortium is a registered charity (number 1097737) funded by the Wellcome Trust, GlaxoSmithKline, Genome Canada, the Canadian Institutes of Health Research, the Ontario Innovation Trust, the Ontario Research and Development Challenge Fund and the Canadian Foundation for Innovation. We thank Martina Leidert and Kristina Rehbein for their contribution to sample preparation and Victoria Higman for help with data analysis.

References

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Copyright information

© Springer Science+Business Media B.V. 2007

Authors and Affiliations

  • Elizabeth F. Dowler
    • 1
  • Annette Diehl
    • 1
  • Peter Schmieder
    • 1
  • Christoph Brockmann
    • 1
  • Jonathan Elkins
    • 2
  • Meera Soundararajan
    • 2
  • Hartmut Oschkinat
    • 1
  • Linda J. Ball
    • 2
  1. 1.Leibniz-Institut für Molekulare Pharmakologie (FMP)BerlinGermany
  2. 2.Structural Genomics Consortium (SGC), Botnar Research CentreUniversity of OxfordOxfordUK

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