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Three-dimensional structure of the actinoporin sticholysin I. Influence of long-distance effects on protein function by Sara García-Linares; Inés Castrillo; Marta Bruix; Margarita Menéndez; Jorge Alegre-Cebollada; Álvaro Martínez-del-Pozo; José G. Gavilanes is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

What is Three-dimensional structure of the actinoporin sticholysin I. Influence of long-distance effects on protein function about?

Actinoporins are water-soluble proteins with the ability to form pores upon insertion into biological membranes. They constitute a family of proteins with high degree of sequence identities but different hemolytic activities, suggesting that minor conformational arrangements result in major functional changes. A good example of this situation is the sea anemone Stichodactyla helianthus which produces two very similar actinoporins, sticholysins I (StnI) and II (StnII), but of very different hemolytic efficiency. Within this idea, given that the high resolution three-dimensional structure of StnII is already known, we have now solved that one corresponding to StnI in order to analyze the influence of particular residues on the conformation and activity of these proteins. In addition, random mutagenesis has been also used to produce five less hemolytic variants of StnI. All these mutations map to functionally relevant regions because they are probably involved in conformational changes associated with pore formation, which take place after membrane binding, and involve long-distance rearrangements of the polypeptide chain of actinoporins.

Who reads Three-dimensional structure of the actinoporin sticholysin I. Influence of long-distance effects on protein function?

It is typically read by researchers, students, and practitioners in Biochemistry, Genetics and Molecular Biology.

Author
Sara García-Linares; Inés Castrillo; Marta Bruix; Margarita Menéndez; Jorge Alegre-Cebollada; Álvaro Martínez-del-Pozo; José G. Gavilanes
Publisher
Elsevier BV
Published
2013
Language
EN
Field
Biochemistry, Genetics and Molecular Biology (Life Sciences)

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