Conserved amino acid residues in ribosome-inactivating proteins from plants

Biochimie. 1991 Jul-Aug;73(7-8):1157-61. doi: 10.1016/0300-9084(91)90160-3.

Abstract

The amino acid sequences of eleven RIPs sequenced to date have been compared in the expectation that this would be useful in the location of functionally and/or structurally important sites of these molecules. In addition to several highly conserved hydrophobic amino acids, thirteen absolutely conserved residues have been found in ricin A-chain: Tyr21, Phe24, Arg29, Tyr80, Tyr123, Gly140, Ala165, Glu177, Ala178, Arg180, Glu208, Asn209 and Trp211. The role of these residues as well as of the C-terminal region have been discussed based on the results of chemical and enzymatic modifications, site-directed mutagenesis, and deletion studies.

MeSH terms

  • Abrin / genetics
  • Amino Acid Sequence
  • Binding Sites
  • Immunotoxins*
  • Lectins / genetics
  • Molecular Sequence Data
  • Mutagenesis, Site-Directed
  • N-Glycosyl Hydrolases*
  • Plant Lectins*
  • Plant Proteins / chemistry
  • Plant Proteins / genetics*
  • Plant Proteins / metabolism
  • Ribosome Inactivating Proteins, Type 1
  • Ribosome Inactivating Proteins, Type 2
  • Ribosomes / metabolism*
  • Ricin / genetics
  • Saporins
  • Sequence Homology, Nucleic Acid
  • Trichosanthin / genetics

Substances

  • Immunotoxins
  • Lectins
  • Plant Lectins
  • Plant Proteins
  • Ribosome Inactivating Proteins, Type 1
  • Ribosome Inactivating Proteins, Type 2
  • Ricinus communis agglutinin-1
  • luffin-a protein, Luffa cylindrica
  • luffin-b protein, Luffa cylindrica
  • Abrin
  • Trichosanthin
  • Ricin
  • N-Glycosyl Hydrolases
  • MAP protein, Mirabilis jalapa
  • Saporins
  • pokeweed antiviral protein