title: New folds of plant lectins.
abstract: Among the crystal structures of lectins determined recently, three--snowdrop lectin, jacalin and amaranthin--represent new lectin families. Their polypeptide folds share remarkably similar features and consist exclusively of beta structure. Autonomously folded beta-sheet subdomains, inter-related by a pseudothreefold symmetry, assemble to form beta-prism or beta-barrel structures which are stabilized by a hydrophobic core.
authors.affiliation: Department of Biochemistry and Molecular Biophysics, Virginia Commonwealth University, Richmond, USA. Christine.Wright@vcu.edu
authors.forename: C S
authors.initials: CS
authors.lastname: Wright
mesh_terms: D019143:Evolution, Molecular; D037102:Lectins / Q000737:chemistry*; D008958:Models, Molecular; D010940:Plant Proteins / Q000737:chemistry*; D011487:Protein Conformation; D017510:Protein Folding; D017433:Protein Structure, Secondary
chemical_list: D037102:Lectins; D010940:Plant Proteins