title: (1)H, (13)C, and (15)N NMR assignments of StnII-R29Q, a defective lipid binding mutant of the sea anemone actinoporin Sticholysin II.
abstract: Several studies have been made to characterize the molecular properties and activity of Sticholysin II (StnII), a 175 amino acid protein secreted by the sea anemone Stichodactyla helianthus. In particular, the biochemical characterization of different mutants of this protein have been shown to be essential for the rational understanding of its activity. Here we report the nearly complete NMR (15)N, (13)C and (1)H chemical shift assignments, at pH 4.0 and 25 degrees C, of a less hemolytic and defective lipid binding mutant of StnII, the R29Q variant (BMRB no 16362).
authors.affiliation: Departamento de Espectroscopía y Estructura Molecular, Instituto de Química Física Rocasolano, CSIC, Madrid, Spain.
authors.forename: Inés
authors.initials: I
authors.lastname: Castrillo
authors.forename: Jorge
authors.initials: J
authors.lastname: Alegre-Cebollada
authors.forename: Alvaro
authors.initials: A
authors.lastname: Martínez-del-Pozo
authors.forename: José G
authors.initials: JG
authors.lastname: Gavilanes
authors.forename: Marta
authors.initials: M
authors.lastname: Bruix
mesh_terms: D000818:Animals; D003064:Cnidarian Venoms / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D017124:Conserved Sequence; D050356:Lipid Metabolism; D050505:Mutant Proteins / Q000737:chemistry* / Q000235:genetics* / Q000378:metabolism; D009154:Mutation; D019906:Nuclear Magnetic Resonance, Biomolecular; D012615:Sea Anemones
chemical_list: D003064:Cnidarian Venoms; D050505:Mutant Proteins; C404794:sticholysin II