Skip to main content
SpringerLink
Log in

1H, 15N, and 13C NMR chemical shift assignments for the Ig3 domain of palladin

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

Abstract

As part of our NMR structure determination of the palladin Ig3 domain, we report nearly complete NMR chemical shift assignments for the 1H, 13C, and 15N nuclei.

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

Fig. 1

Similar content being viewed by others

References

  • Boukhelifa M, Moza M, Johansson T, Rachlin A, Parast M, Huttelmaier S, Roy P, Jockusch BM, Carpen O, Karlsson R, Otey CA (2006) The proline-rich protein palladin is a binding partner for profilin. FEBS J 273:26–33

    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 

  • Dixon RDS, Arneman DK, Rachlin AS, Sundaresan N, Joseph Costello M, Campbell SL, Otey CA (2008) Palladin is an actin crosslinking protein that uses immunoglobulin-like domains to bind filamentous actin. J Biol Chem 283(10):6222–6231

    Article  Google Scholar 

  • Johnson BA (2004) Using NMRView to visualize and analyze the NMR spectra of macromolecules. Methods Mol Biol 278:313–352

    Google Scholar 

  • Otey CA, Rachlin A, Moza M, Arneman D, Carpen O (2005) The palladin/myotilin/myopalladin family of actin-associated scaffolds. Int Rev Cytol 246:31–58

    Article  Google Scholar 

  • Parast MM, Otey CA (2000) Characterization of palladin, a novel protein localized to stress fibers and cell adhesions. J Cell Biol 150:643–656

    Article  Google Scholar 

  • Rachlin AS, Otey CA (2006) Identification of palladin isoforms and characterization of an isoform-specific interaction between Lasp-1 and palladin. J Cell Sci 119:995–1004

    Article  Google Scholar 

  • Slupsky CM, Boyko RF, Booth VK, Sykes BD (2003) Smartnotebook: a semi-automated approach to protein sequential NMR resonance assignments. J Biomol NMR 27:313–321

    Article  Google Scholar 

  • Wishart DS, Sykes BD (1994) The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data. J Biomol NMR 4:171–180

    Article  Google Scholar 

  • Wishart DS, Bigam CG, Yao J, Abildgaard F, Dyson HJ, Oldfield E, Markley JL, Sykes BD (1995) 1H, 13C and 15N chemical shift referencing in biomolecular NMR. J Biomol NMR 6:135–140

    Article  Google Scholar 

Download references

Acknowledgements

Support for this work was provided by the National Institutes of Health NS43253. We would like to thank Greg Young, the NMR facility manager at UNC-CH, for his assistance in NMR data collection. Dr. Kirk Prutzman and Dr. Yibing Wu both provided helpful suggestions for data collection and analysis. We acknowledge Andrew Rachlin, who while working in the laboratory of Dr. Carol Otey at UNC-CH, cloned the palladin Ig3 domain and constructed the modified pMAL-c2x vector.

Author information

Authors and Affiliations

  1. Department of Biochemistry and Biophysics, The University of North Carolina at Chapel Hill, Chapel Hill, NC, 27599, USA

    Richard D. S. Dixon & Sharon L. Campbell

  2. The Lineberger Comprehensive Cancer Center, The University of North Carolina at Chapel Hill, Chapel Hill, NC, 27599, USA

    Sharon L. Campbell

Authors
  1. Richard D. S. Dixon
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Sharon L. Campbell
    View author publications

    You can also search for this author in PubMed Google Scholar

Corresponding author

Correspondence to Sharon L. Campbell.

Rights and permissions

Reprints and permissions

About this article

Cite this article

Dixon, R.D.S., Campbell, S.L. 1H, 15N, and 13C NMR chemical shift assignments for the Ig3 domain of palladin. Biomol NMR Assign 2, 51–53 (2008). https://doi.org/10.1007/s12104-008-9082-z

Download citation

  • Received:

  • Accepted:

  • Published:

  • Issue Date:

  • DOI: https://doi.org/10.1007/s12104-008-9082-z

Keywords

Search

Navigation