Literature DB >> 19636934

1H, 13C, and 15N NMR assignments of the actinoporin Sticholysin I.

Inés Castrillo1, Jorge Alegre-Cebollada, Alvaro Martínez del Pozo, José G Gavilanes, Jorge Santoro, Marta Bruix.   

Abstract

Sticholysin I is an actinoporin, a pore forming toxin, of 176 aminoacids produced by the sea anemone Stichodactyla heliantus. Isotopically labelled (13)C/(15)N recombinant protein was produced in E. coli. Here we report the complete NMR (15)N, (13)C and (1)H chemical shifts assignments of Stn I at pH 4.0 and 25 degrees C (BMRB No. 15927).

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Year:  2008        PMID： 19636934     DOI： 10.1007/s12104-008-9127-3

Source DB:  PubMed          Journal:  Biomol NMR Assign        ISSN： 1874-270X            Impact factor:   0.746


  2 in total

1.  The membranotropic activity of N-terminal peptides from the pore-forming proteins sticholysin I and II is modulated by hydrophobic and electrostatic interactions as well as lipid composition.

Authors:  Uris Ros; Lohans Pedrera; DaylÍn Diaz; Juan C De Karam; Tatiane P Sudbrack; Pedro A Valiente; Diana MartÍnez; Eduardo M Cilli; Fabiola Pazos; Rosangela Itri; Maria E Lanio; Shirley Schreier; Carlos Ávarez
Journal:  J Biosci       Date:  2011-12       Impact factor: 1.826

2.  Self-homodimerization of an actinoporin by disulfide bridging reveals implications for their structure and pore formation.

Authors:  Aisel Valle; Luis Benito Pérez-Socas; Liem Canet; Yadira de la Patria Hervis; German de Armas-Guitart; Diogo Martins-de-Sa; Jônatas Cunha Barbosa Lima; Adolfo Carlos Barros Souza; João Alexandre Ribeiro Gonçalves Barbosa; Sonia Maria de Freitas; Isabel Fabiola Pazos
Journal:  Sci Rep       Date:  2018-04-26       Impact factor: 4.379
  2 in total

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