title: Lectins.
abstract: Lectins - carbohydrate-binding proteins involved in a variety of recognition processes - exhibit considerable structural diversity. Three new lectin folds and further elaborations of known folds have been described recently. Large variability in quaternary association resulting from small alterations in essentially the same tertiary structure is a property exhibited specially by legume lectins. The strategies used by lectins to generate carbohydrate specificity include the extensive use of water bridges, post-translational modification and oligomerization. Recent results pertaining to influenza and foot-and-mouth viruses further elaborate the role of lectins in infection.
authors.affiliation: Molecular Biophysics Unit, Indian Institute of Science, Bangalore, 560 012, India. mv@mbu.iisc.ernet.in
authors.forename: M
authors.initials: M
authors.lastname: Vijayan
authors.forename: N
authors.initials: N
authors.lastname: Chandra
mesh_terms: D050260:Carbohydrate Metabolism; D029544:Foot-and-Mouth Disease Virus / Q000737:chemistry*; D037102:Lectins / Q000737:chemistry* / Q000378:metabolism; D008958:Models, Molecular; D009975:Orthomyxoviridae / Q000737:chemistry*; D017510:Protein Folding; D020836:Protein Structure, Quaternary
chemical_list: D037102:Lectins