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Editing and expanding the article: Rib osome-inactivating protein.

Plan to add information of the different types of ribosome-inactivating proteins.

Ribosome-inactivating proteins (RIPs) are separated into three types based on protein domain composition:


 * Type I: RIPs-I are polypeptides composed of an A domain. This is the site of N-glycosidase activity.
 * Type II: RIPs-II are composed of an A domain with similar catalytic activity to Type I RIPs, and a B domain with lectin-binding properties. These properties facilitate entry into the cell, thus making Type II particularly cytotoxic. The A and B domains are fused together by disulfide bonds.
 * RIPs-II are considered potent toxins. The B domain is able to bind galactosyl moieties on the cell surface which facilitates entry into the cell, where the A domain can perform its catalytic activity on 28S rRNA in the cytosol.
 * Type III: RIPs-III are separated into two subgroups. One subgroup contains the same original RIP domain (A), and a C-terminal with unknown functionality. The other subgroup is similar to Type I, but contains a site for inactivation.