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

The Trp111 to Cys mutant of sticholysin I, an actinoporin from Stichodactyla helianthus sea anemone, forms a homodimer via a disulfide bridge. The purified dimer is 193 times less hemolytic than the monomer. Ultracentrifugation, dynamic light scattering and size-exclusion chromatography demonstrate...

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Detalles Bibliográficos
Autores principales: Valle, Aisel, Pérez-Socas, Luis Benito, Canet, Liem, Hervis, Yadira de la Patria, de Armas-Guitart, German, Martins-de-Sa, Diogo, Lima, Jônatas Cunha Barbosa, Souza, Adolfo Carlos Barros, Barbosa, João Alexandre Ribeiro Gonçalves, de Freitas, Sonia Maria, Pazos, Isabel Fabiola
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2018
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5920107/
https://www.ncbi.nlm.nih.gov/pubmed/29700324
http://dx.doi.org/10.1038/s41598-018-24688-2

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