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Biomolecular NMR Assignments

, Volume 7, Issue 1, pp 25–29 | Cite as

1H, 13C, and 15N chemical shifts assignments for human endothelial monocyte-activating polypeptide EMAP II

  • Dmytro Lozhko
  • Jan Stanek
  • Krzysztof Kazimierczuk
  • Anna Zawadzka-Kazimierczuk
  • Wiktor Kozminski
  • Igor Zhukov
  • Alexander Kornelyuk
Article

Abstract

Endothelial and monocyte-activating polypeptide II (EMAP II) is a cytokine that plays an important role in inflammation, apoptosis and angiogenesis processes in tumour tissues. Structurally, the EMAP II is a 169 amino acid residues long C-terminal domain (residues 147–312) of auxiliary tRNA binding protein p43. In spite of existence in pdb databank of two X-ray structures there are some important aspects of EMAP II cytokine function which are still not fully understood in detail. To obtain information about 3D structure and backbone dynamic processes in solution we perform structure evaluation of human EMAP II cytokine by NMR spectroscopy. The standard approach to sequence-specific backbone assignment using 3D NMR data sets was not successful in our studies and was supplemented by recently developed 4D NMR experiments with random sampling of evolution time space. Here we report the backbone and side chain 1H, 13C, and 15N chemical shifts in solution for recombinant EMAP II cytokine together with secondary structure provided by TALOS + software.

Keywords

Multidimensional NMR spectroscopy Random sampling Sequence-specific backbone assignment Side chain assignments Cytokines EMAP II 

Notes

Acknowledgments

This work was partially supported by grant N 30107131/2150 from Polish Ministry of Sciences and High Education, and FP7 EastNMR project (contract no. 228461) inside of transnational access program (for D.L. and A.K.). This work was performed as a JRA activity in FP7 BioNMR project (contract no. 261863) between Slovenian NMR Centre and Faculty of Chemistry, University of Warsaw. A.Z.-K. thanks the Foundation for Polish Science for supporting her with the MPD Programme, KK and WK thanks the Foundation for Polish Science for support with the TEAM Programme. MPD and TEAM programmes were co-financed by the EU European Regional Development.

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Copyright information

© Springer Science+Business Media B.V. 2012

Authors and Affiliations

  • Dmytro Lozhko
    • 1
  • Jan Stanek
    • 2
  • Krzysztof Kazimierczuk
    • 2
  • Anna Zawadzka-Kazimierczuk
    • 2
  • Wiktor Kozminski
    • 2
  • Igor Zhukov
    • 3
    • 4
    • 5
  • Alexander Kornelyuk
    • 1
  1. 1.Institute Molecular Biology and Genetics, National Academy of Sciences of UkraineKyivUkraine
  2. 2.Faculty of ChemistryUniversity of WarsawWarsawPoland
  3. 3.Slovenian NMR CentreNational Institute of ChemistryLjubljanaSlovenia
  4. 4.EN-FIST Center of ExcellenceLjubljanaSlovenia
  5. 5.Institute of Biochemistry and Biophysics, Polish Academy of SciencesWarsawPoland

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