Abstract: Basic 7S globulin and leginsulin are widely distributed in legume species and play role in growth and development of legumes by a mechanism similar to the insulin regulatory pathway in animals. Basic 7S globulin is a cysteine-rich glycoprotein and has tyrosine kinase activity. It has some structural similarities with human insulin receptor and can bind with insulin and insulin-like growth factor Ⅰ and Ⅱ. Leginsulin and PA1b are polypeptides consisting of 37 amino acid residues with 6 cysteines in 3 disulfide bridges, both belonging to the cysteine-knot family. PA1b was the first entomotoxic cysteine-knot peptide identified and found to have single binding site in weevil, pea aphid and fruit fly. Magnetic resonance imaging studies showed topological similarity of critical residues between leginsulin and insulin. Research progress on the structure and physiological function of basic 7S globulin and leginsulin is reviewed.

Key words: Basic 7S globulin, Leginsulin, Structural trait, Physiological function