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Aminopeptidase N-receptor

Figure 7.30 Mode of action of Cry toxins. (a,b) Crystals are solubilized and activated to give rise to the monomeric toxin, (c) The toxin monomer binds in cadherin receptor, followed by proteolytic cleavage of helix a-1. (d) The tetramer is formed by inter monomeric contacts, (e) The toxin oligomer binds to the aminopeptidase-N receptor (APN receptor). The APN receptor and oligomeric Cry toxin localize to lipid rafts, (f) Following a conformational change, the oligomer inserts into membrane, forming a tetrameric pore. (From Bravo et al., in Comprehensive Molecular Insect Science, Gilbert, L.I., Iatrou, K., and Gill, S.S., Eds., Vol. 6, Elsevier, London, 2005, p. 175. With permission.)... Figure 7.30 Mode of action of Cry toxins. (a,b) Crystals are solubilized and activated to give rise to the monomeric toxin, (c) The toxin monomer binds in cadherin receptor, followed by proteolytic cleavage of helix a-1. (d) The tetramer is formed by inter monomeric contacts, (e) The toxin oligomer binds to the aminopeptidase-N receptor (APN receptor). The APN receptor and oligomeric Cry toxin localize to lipid rafts, (f) Following a conformational change, the oligomer inserts into membrane, forming a tetrameric pore. (From Bravo et al., in Comprehensive Molecular Insect Science, Gilbert, L.I., Iatrou, K., and Gill, S.S., Eds., Vol. 6, Elsevier, London, 2005, p. 175. With permission.)...
Jenkins, J.L., M.K. Lee, S. Sangadala, M.J. Adang, and D.H. Dean. 1999. Binding of Bacillus thuringiensis Cryl Ac toxin to Manduca sexta aminopeptidase-N receptor is not directly related to toxicity. FEBS Lett. 462 373-376. [Pg.264]

Bacillus thuringiensis toxin to gypsy moth aminopeptidase N receptor. J. Biol. Chem. 275 14423-14431. [Pg.264]

See other pages where Aminopeptidase N-receptor is mentioned: [Pg.279]   
See also in sourсe #XX -- [ Pg.135 ]



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