Biomolecular NMR Assignments

, Volume 7, Issue 1, pp 65–67 | Cite as

1H, 13C, and 15N resonance assignments of the second immunoglobulin domain of neurolin from Carassius auratus

  • Žarko Kulić
  • Günter Fritz
  • Heiko M. MöllerEmail author


Neurolin is a member of the superfamily of immunoglobulin-like cell surface receptors. It is essential during neuronal development in the model organism Carassius auratus (goldfish) and involved in the guidance of the growing axon. Among the five extracellular immunoglobulin (Ig) domains, the second Ig domain is crucial for axon pathfinding. In the present study, we report the NMR assignment and secondary structure prediction of the second Ig domain of neurolin.


Neurolin Goldfish Neuronal receptor Axonal pathfinding 



We thank Prof. Dr. Claudia Stürmer for continuous support and helpful discussion. The plasmid for the ULP1 protease was kindly provided by Prof. Dr. Elke Deuerling and her coworker Dr. Steffen Preissler. We are grateful for expert technical assistance by Anke Friemel during setup of NMR experiments. Financial support by the Konstanz Research School Chemical Biology (KoRS-CB) including a PhD fellowship to Ž. Kulić, and by the Young Scholar Fund of the University of Konstanz is gratefully acknowledged. Günter Fritz is supported by a Heisenberg fellowship of the Deutsche Forschungsgemeinschaft (FR 1488/3-1).


  1. Bax A, Subramanian J (1986) Sensitivity-enhanced two-dimensional heteronuclear shift correlation NMR spectroscopy. J Magn Reson 67(3):565–570Google Scholar
  2. Denzinger T, Diekmann H, Bruns K, Laessing U, Stuermer CA, Przybylski M (1999) Isolation, primary structure characterization and identification of the glycosylation pattern of recombinant goldfish neurolin, a neuronal cell adhesion protein. J Mass Spectrom 34(4):435–446CrossRefGoogle Scholar
  3. Inoue H, Nojima H, Okayama H (1990) High efficiency transformation of Escherichia coli with plasmids. Gene 96(1):23–28CrossRefGoogle Scholar
  4. Keller R (2004) The computer aided resonance assignment tutorial. CANTINA Verlag, GoldauGoogle Scholar
  5. Leppert CA, Diekmann H, Paul C, Laessing U, Marx M, Bastmeyer M, Stuermer CA (1999) Neurolin Ig domain 2 participates in retinal axon guidance and Ig domains 1 and 3 in fasciculation. J Cell Biol 144(2):339–349CrossRefGoogle Scholar
  6. Malakhov MP, Mattern MR, Malakhova OA, Drinker M, Weeks SD, Butt TR (2004) SUMO fusions and SUMO-specific protease for efficient expression and purification of proteins. J Struct Funct Genomics 5(1):75–86CrossRefGoogle Scholar
  7. Paschke KA, Lottspeich F, Stuermer CA (1992) Neurolin, a cell surface glycoprotein on growing retinal axons in the goldfish visual system, is reexpressed during retinal axonal regeneration. J Cell Biol 117(4):863–875CrossRefGoogle Scholar
  8. Shen Y, Delaglio F, Cornilescu G, Bax A (2009) TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts. J Biomol NMR 44(4):213–223CrossRefGoogle Scholar
  9. Stuermer CA, Bastmeyer M (2000) The retinal axon’s pathfinding to the optic disk. Prog Neurobiol 62(2):197–214CrossRefGoogle Scholar
  10. Wade A, Thomas C, Kalmar B, Terenzio M, Garin J, Greensmith L, Schiavo G (2012) Activated Leukocyte Cell Adhesion Molecule (Alcam) modulates neurotrophin signaling. J Neurochem [Epub ahead of print]. doi: 10.1111/j.1471-4159.2012.07658.x
  11. 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(2):135–140CrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media B.V. 2012

Authors and Affiliations

  • Žarko Kulić
    • 1
  • Günter Fritz
    • 2
  • Heiko M. Möller
    • 1
    Email author
  1. 1.Department of Chemistry and Konstanz Research School Chemical BiologyUniversity of KonstanzKonstanzGermany
  2. 2.Department of NeuropathologyUniversity of FreiburgFreiburgGermany

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