Structural foundations of sticholysin functionality
نویسندگان
چکیده
Actinoporins constitute a family of α pore-forming toxins produced by sea anemones. The soluble fold these proteins consists β-sandwich flanked two α-helices. exert their activity specifically recognizing sphingomyelin at target membranes. Once there, they penetrate the membrane with N-terminal α-helices, process that leads to formation cation-selective pores. These pores kill cells provoking an osmotic shock on them. In this review, we examine role and relevance structural features actinoporins, down residue level. We look specific amino acids play significant roles in function actinoporins fold. Particular emphasis is given those residues display high degree conservation across actinoporin sequences known date. light latest findings field, requirements for pore formation, effect lipid composition, are also discussed.
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ژورنال
عنوان ژورنال: Biochimica Et Biophysica Acta - Proteins And Proteomics
سال: 2021
ISSN: ['0926-6569', '1878-1454', '1878-223X', '0167-4838', '0005-2795', '1570-9639', '1879-2952', '0926-6593', '1878-2248', '1879-2588', '0005-2744']
DOI: https://doi.org/10.1016/j.bbapap.2021.140696