[Ribosome-inactivating lectins from plants].
There is a heterogeneous group of plant proteins which are able to enzymatically inactivate ribosomes by depurination of an invariant adenine from the 28 S ribosomal RNA. Some of these proteins are heterodimers having a lectin subunit which is joined by disulfide bond to the enzymatic subunit. Ricin and abrin which are among the most toxic substances known belong to the last group. This review focuses on the structure of the heterodimeric plant ribosome-inactivating proteins, the way of their action on ribosome, biosynthesis, intracellular trafficking, and their possible usage in medicine.
Kozlov
Iu V
IuV
Sudarkina
O Iu
OIu
Kurmanova
A G
AG
D000036:Abrin / Q000378:metabolism / Q000494:pharmacology; D000595:Amino Acid Sequence; D000818:Animals; D008969:Molecular Sequence Data; D037121:Plant Lectins / Q000378:metabolism* / Q000633:toxicity; D014176:Protein Biosynthesis / Q000187:drug effects / Q000502:physiology*; D011500:Protein Synthesis Inhibitors / Q000494:pharmacology; D021381:Protein Transport; D012338:RNA, Ribosomal, 23S / Q000378:metabolism; D012270:Ribosomes / Q000187:drug effects / Q000502:physiology*; D012276:Ricin / Q000378:metabolism / Q000494:pharmacology; D017386:Sequence Homology, Amino Acid
D037121:Plant Lectins; D011500:Protein Synthesis Inhibitors; D012338:RNA, Ribosomal, 23S; D000036:Abrin; D012276:Ricin