Taxonomic distribution of proteins containing RICIN domains

The RICIN domain within your query sequence starts at position 40 and ends at position 160, and its E-value is 8.49e-12.

The (QxW)3 domain: a flexible lectin scaffold.

Hazes B
Protein Sci. 1996; 5: 1490-501

Lectins form a class of proteins that have evolved a specialized carbohydrate-binding function. Based on amino acid sequence analysis, several lectin families have been described and a lectin domain, the (QxW)3 domain, was discussed recently based on 11 family members. In this paper, the (QxW)3 domain family is extended to 45 sequences, several of which have very low sequence identity with the previously known members of the family. A hidden Markov model was used to identify the most divergent members of the family. The expanded set of sequences gives us a more complete appreciation of the conserved features, and the lack thereof, in this lectin family. This, in turn, provides new insights in the structural and functional properties of the individual family members.

Structural evolution of the annexin supergene family.

Smith PD, Moss SE
Trends Genet. 1994; 10: 241-6

The annexin family of calcium-binding proteins is comprised of at least ten mammalian genes, with additional representatives in lower eukaryotes. Recent structural analyses of several annexin genes have provided insights into the relationship between exon organization and functional domains. We discuss the implications of these findings and speculate on the evolutionary origins of the annexin supergene family.

The structure and action of ricin, a cytotoxic N-glycosidase.

Robertus J
Semin Cell Biol. 1991; 2: 23-30

The X-ray structure of the heterodimeric plant cytotoxin ricin has been elucidated. The A chain, known to be a specific N-glycosidase, has a prominent active site cleft. The B chain is a two domain lectin, which arose from the replication of a primitive sugar binding peptide. The molecular model reveals residues which are likely to be important in the action of the protein. Site directed mutagenesis reveals the relative importance of a number of these groups. A model for the mechanism of the A chain, including steric strain of the scissile bond and carboxonium ion transition state stabilization is proposed.

Structure and evolution of ricin B chain.

Rutenber E, Ready M, Robertus JD
Nature. 1987; 326: 624-6

Ricin is a dimeric toxin from the castor bean Ricinus communis, which is composed of a sugar-binding subunit (B) that attaches to receptors on the surfaces of target cells and a subunit (A) with enzymatic activity that attacks and inactivates ribosomes. We report here that comparison of amino-acid sequence data with high-resolution structure analysis of the ricin B subunit shows it to be the product of a series of gene duplications. The modern protein has two sugar-binding domains, each of which is composed of three copies of a more ancient galactose-binding peptide of about 40 residues.

Ricin B chain is a product of gene duplication.

Villafranca JE, Robertus JD
J Biol Chem. 1981; 256: 554-6

The cytotoxin ricin is a heterodimer composed of an A chain which enzymatically inhibits protein synthesis on eukaryotic ribosomes and a lectin B chain which binds to cell surfaces and triggers uptake of the toxin. A low resolution (4 A) x-ray structure revealed that the B chain is a bilobal structure and that each domain binds a galactose sugar. These apparent structural similarities suggested that the protein might have internal symmetry and might have arisen by gene duplication. A subsequent search of the amino acid sequence provided strong evidence for homology between th NH2- and COOH-terminal halves of the B chain and suggested that they may have arisen from a common ancestor. There is no strong relationship between the halves of the A chain and little, if any, significant sequence homology between the A and B chains of ricin.