Rapid Topology Determination of Membrane Proteins: Pore-Forming Mechanism of Bt toxin Cry1Aa
نویسندگان
چکیده
منابع مشابه
Rapid topology probing using fluorescence spectroscopy in planar lipid bilayer: the pore-forming mechanism of the toxin Cry1Aa of Bacillus thuringiensis
Pore-forming toxins, many of which are pathogenic to humans, are highly dynamic proteins that adopt a different conformation in aqueous solution than in the lipid environment of the host membrane. Consequently, their crystal structures obtained in aqueous environment do not reflect the active conformation in the membrane, making it difficult to deduce the molecular determinants responsible for ...
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Y. Tanaka and M. Yao (Hokkaido Univ.) Pathogenic bacteria express pore-forming toxins (PFTs) to attack host cells. PFTs are expressed as soluble monomeric proteins, which assemble to prepore oligomer on the target cells. After forming prepore, conformational change occurs, and then the pore is formed. Although the crystal structures of monomer and pore have been determined, the detailed mechani...
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The human pathogen Streptococcus pneumoniae produces soluble pneumolysin monomers that bind host cell membranes to form ring-shaped, oligomeric pores. We have determined three-dimensional structures of a helical oligomer of pneumolysin and of a membrane-bound ring form by cryo-electron microscopy. Fitting the four domains from the crystal structure of the closely related perfringolysin reveals ...
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Objective(s): Current therapeutic strategies for cancer are associated with side effects and lack of specificity in treatments. Biological therapies including monoclonal antibodies and immune effectors have been the subject of multiple research projects. Pore-forming proteins may become the other biological strategy to overcome the problems associated with current treatments. But detailed mecha...
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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 2009
ISSN: 0006-3495
DOI: 10.1016/j.bpj.2008.12.2761