Non-carbohydrate binding partners/domains of animal lectins.
1. Protein-carbohydrate interactions are involved in a large number of biologically important recognition processes. 2. Among the participating classes of proteins lectins are defined as carbohydrate-binding proteins other than an antibody or an enzyme. 3. In addition to the essential carbohydrate-binding domain other functionally and/or structurally important sites, defined by sequence comparison or by experimental demonstration of protein-protein interactions, can be present within the lectin molecule and may be relevant for its physiological significance. 4. Sequence motifs of lectins for protein-protein interactions include amino acid structures designed for cell adhesion, growth regulatory biosignalling, intracellular routing and enzymatic activity. 5. Elucidation of the complete functional role(s) of a lectin requires accurate delineation of its carbohydrate and, if present, of its protein ligands. 6. Presence of more than one carbohydrate-binding domain in a single lectin, potential ligand properties of the glycopart of a lectin, regulatory interplay between different sites and possible interaction of complementarily shaped peptide sequences to the sugar-recognizing site should all be assessed in the quest to comprehensively explain the physiological role(s) of a lectin.
Institut für Physiologische Chemie, Ludwig-Maximilians-Universität, München, Germany.
H J
HJ
Gabius
D000595:Amino Acid Sequence; D000818:Animals; D001665:Binding Sites; D050260:Carbohydrate Metabolism; D049672:History, 19th Century; D049673:History, 20th Century; D006801:Humans; D037102:Lectins / Q000737:chemistry / Q000266:history / Q000378:metabolism*; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000737:chemistry / Q000378:metabolism; D011485:Protein Binding
D037102:Lectins; D009842:Oligopeptides; C047981:arginyl-glycyl-aspartic acid