Funatsu G, Islam M R, Minami Y, Sung-Sil K, Kimura M
Laboratory of Protein Chemistry and Engineering, Faculty of Agriculture, Kyushu University, Fukuoka, Japan.
Biochimie. 1991 Jul-Aug;73(7-8):1157-61. doi: 10.1016/0300-9084(91)90160-3.
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.
