Author: Shapira, Assaf; Benhar, Itai
Title: Toxin-Based Therapeutic Approaches Document date: 2010_10_28
ID: 00cf294x_16_1
Snippet: e bond, the enzymatically active C terminal fragment, which is composed of domain III and about two thirds of domain II, is routed to the trans-Golgi network where it binds via its C terminally exposed REDL sequence to KDEL receptor and travels to the endoplasmic reticulum (ER); 6. In the ER, sequences in domain II mediate the retro-translocation of the polypeptide via the Sec61p translocon into the cytoplasm; 7. The catalytic domain inactivates .....
Document: e bond, the enzymatically active C terminal fragment, which is composed of domain III and about two thirds of domain II, is routed to the trans-Golgi network where it binds via its C terminally exposed REDL sequence to KDEL receptor and travels to the endoplasmic reticulum (ER); 6. In the ER, sequences in domain II mediate the retro-translocation of the polypeptide via the Sec61p translocon into the cytoplasm; 7. The catalytic domain inactivates eukaryotic translation elongation factor 2 (eEF2) by ADP-ribosylation, which causes translation inhibition and consequently cell death. For the construction of PE-based immunotoxins, the receptor binding domain Ia can be replaced by an antibody, antibody derivative, or a ligand, which preferentially binds to tumor-associated antigen/receptor. The resulting truncated form of PE is designated PE40, indicating its molecular weight (40 kDa). In addition, a large part of domain Ib can be deleted without effecting cytotoxicity, generating a smaller form of the modified toxin, which is denoted PE38 (38 kDa).
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