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Hydropathic complementarity determines interaction of epitope (869)HITDTNNK(876) in Manduca sexta Bt-R(1) receptor with loop 2 of domain II of Bacillus thuringiensis Cry1A toxins.
Gomez I, Miranda-Rios J, Rudiño-Piñera E, Oltean DI, Gill SS, Bravo A, Soberón M. Gomez I, et al. J Biol Chem. 2002 Aug 16;277(33):30137-43. doi: 10.1074/jbc.M203121200. Epub 2002 Jun 5. J Biol Chem. 2002. PMID: 12050155 Free article.
The CDR3 region of scFv73 shared homology with an 8-amino acid epitope ((869)HITDTNNK(876)) of the Manduca sexta cadherin-like receptor Bt-R(1) (Gomez, I., Oltean, D. I., Gill, S. S., Bravo, A., and Soberon, M. (2001) J. ...
The CDR3 region of scFv73 shared homology with an 8-amino acid epitope ((869)HITDTNNK(876)) of the Manduca sexta cadherin-like receptor Bt-R …
Molecular basis for Bacillus thuringiensis Cry1Ab toxin specificity: two structural determinants in the Manduca sexta Bt-R1 receptor interact with loops alpha-8 and 2 in domain II of Cy1Ab toxin.
Gómez I, Dean DH, Bravo A, Soberón M. Gómez I, et al. Biochemistry. 2003 Sep 9;42(35):10482-9. doi: 10.1021/bi034440p. Biochemistry. 2003. PMID: 12950175
In previous works, we determined that the Manduca sexta Cry1A cadherin-like receptor (Bt-R(1)) interacts with Cry1A toxins through epitope (865)NITIHITDTNN(875) and by loop 2 of domain II in the toxin (Gomez, I., Miranda-Rios, J., Rudino-Pinera, E., Oltean, D. I
In previous works, we determined that the Manduca sexta Cry1A cadherin-like receptor (Bt-R(1)) interacts with Cry1A toxins through epitope ( …
Oligomerization triggers binding of a Bacillus thuringiensis Cry1Ab pore-forming toxin to aminopeptidase N receptor leading to insertion into membrane microdomains.
Bravo A, Gómez I, Conde J, Muñoz-Garay C, Sánchez J, Miranda R, Zhuang M, Gill SS, Soberón M. Bravo A, et al. Among authors: gomez i. Biochim Biophys Acta. 2004 Nov 17;1667(1):38-46. doi: 10.1016/j.bbamem.2004.08.013. Biochim Biophys Acta. 2004. PMID: 15533304 Free article.
Toxin monomeric structure binds to Bt-R1, a cadherin-like protein, that induces proteolytic processing and oligomerization of the toxin (Gomez, I., Sanchez, J., Miranda, R., Bravo A., Soberon, M., FEBS Lett. (2002) 513, 242-246), while the oligomeric structure binds …
Toxin monomeric structure binds to Bt-R1, a cadherin-like protein, that induces proteolytic processing and oligomerization of the toxin ( …
683 results