title: (1)H, (13)C, and (15)N resonance assignments of the second immunoglobulin domain of neurolin from Carassius auratus.
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.
authors.affiliation: Department of Chemistry and Konstanz Research School Chemical Biology, University of Konstanz, Universitätsstraße 10, 78457, Konstanz, Germany.
authors.forename: Žarko
authors.initials: Ž
authors.lastname: Kulić
authors.forename: Günter
authors.initials: G
authors.lastname: Fritz
authors.forename: Heiko M
authors.initials: HM
authors.lastname: Möller
mesh_terms: D020410:Activated-Leukocyte Cell Adhesion Molecule / Q000737:chemistry*; D000818:Animals; D029941:Fish Proteins / Q000737:chemistry*; D006054:Goldfish; D007136:Immunoglobulins / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular; D017434:Protein Structure, Tertiary
chemical_list: D020410:Activated-Leukocyte Cell Adhesion Molecule; D029941:Fish Proteins; D007136:Immunoglobulins