Ricin Structure

Ricin (accounting for about 5% of ricin, with a molecular weight of about 66 kD) is a type II heterodimeric ribosome inactivating protein, which is composed of ribosome inactivating enzymes (ricin A chain) and half Lactose/N-acetylgalactosamine is composed of a lectin (ricin B chain) specifically bound, and a disulfide bond is connected between the two. The analysis of the primary structure of ricin found that the A chain contains 267 amino acid residues with a molecular weight of about 32 kD. It has catalytic activity and is the effector chain of ricin protein. A lysine (Lys) residue is contained in the 4th position of the N-terminal and the C-terminal of the A chain, which is the key center of the toxic effect of the ricin A chain. The B chain has 2 domains, these 2 domains have homology and are produced by gene duplication. Domain 1 contains the amino terminus, while domain 2 contains the carboxy terminus. Ricin B chain is composed of 267 amino acid residues and has binding activity. It is the binding chain of ricin.