Abstract
Sticholysin II is an actinoporin of 175 amino acids produced by the sea anemone Stichodactyla helianthus. Several studies with different mutants have been performed to characterize its molecular properties and activity. As a first step towards a 3D structural characterization and its interaction with membrane models at a residue level, herein we report the nearly complete NMR 15N, 13C and 1H chemical shifts assignments of the Y111N variant at pH 4.0 and 25°C (BMRB No. 16630). The assignment is complete for the biologically relevant residues, specially for those implicated in membrane interactions.
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Acknowledgments
This paper was supported by projects CTQ2008-00080/BQU and BFU2006-04404 from the Spanish Ministerio de Ciencia e Innovación.
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Pardo-Cea, M.A., Alegre-Cebollada, J., Martínez-del-Pozo, Á. et al. 1H, 13C, and 15N NMR assignments of StnII-Y111N, a highly impaired mutant of the sea anemone actinoporin Sticholysin II. Biomol NMR Assign 4, 69–72 (2010). https://doi.org/10.1007/s12104-010-9214-0
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DOI: https://doi.org/10.1007/s12104-010-9214-0