RT Journal Article
T1 Three-dimensional structure of the actinoporin sticholysin I. Influence of long-distance effects on protein function
A1 García Linares, Sara
A1 Castrillo, Inés
A1 Bruix, Marta
A1 Menéndez, Margarita
A1 Alegre-Cebollada, Jorge
A1 Martínez Del Pozo, Álvaro
A1 Gavilanes Franco, José Gregorio
AB 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.
PB Elsevier
SN 0003-9861
YR 2013
FD 2013
LK https://hdl.handle.net/20.500.14352/97736
UL https://hdl.handle.net/20.500.14352/97736
LA eng
NO García-Linares, Sara, et al. «Three-Dimensional Structure of the Actinoporin Sticholysin I. Influence of Long-Distance Effects on Protein Function». Archives of Biochemistry and Biophysics, vol. 532, n.o 1, abril de 2013, pp. 39-45. https://doi.org/10.1016/j.abb.2013.01.005
NO Ministerio de Ciencia e Innovación (España)
DS Docta Complutense
RD 7 abr 2025