Abstract
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.
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Acknowledgments
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).
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Kulić, Ž., Fritz, G. & Möller, H.M. 1H, 13C, and 15N resonance assignments of the second immunoglobulin domain of neurolin from Carassius auratus . Biomol NMR Assign 7, 65–67 (2013). https://doi.org/10.1007/s12104-012-9379-9
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DOI: https://doi.org/10.1007/s12104-012-9379-9